New Products

New Products

Our extensive selection of Cytokine, Antibody, ELISA, and Media products is continuously expanding to address your current research interests.

Here you can find a list of our newly released products.

New

Size

95.00 USD 10µg
215.00 USD 50µg
330.00 USD 100µg
577.50 USD 250µg
990.00 USD 500µg
1,650.00 USD 1mg
Looking for a custom size?
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Animal-Free Recombinant Human Apo-SAA1

Serum amyloid A proteins (SAA) represents a family of apolipoproteins that circulates in association with high-density lipoproteins (HDL). The level of Apo-SAA, normally 1-5 μg/ml in plasma, increases 500-1000 fold within 24 hours of an inflammatory stimulus and, under these conditions, is the most abundant HDL apolipoprotein. The human SAA gene codes for a 122 amino acid nonglycosylated polypeptide, which contains an 18 amino acid N-terminal sequence. Recombinant Human Apo-SAA1 is an 11.7 kDa protein containing 105 amino acid residues.

Manufactured using all Animal-Free reagents.

Source: E.coli

Synonyms: None

AA Sequence: MRSFFSFLGE AFDGARDMWR AYSDMREANY IGSDKYFHAR GNYDAAKRGP GGVWAAEAIS DARENIQRFF GHGAEDSLAD QAANEWGRSG KDPNHFRPAG LPEKY

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to chemoattract human monocytes using a concentration range of 10.0-100.0 ng/ml.

New

Size

95.00 USD 10µg
215.00 USD 50µg
330.00 USD 100µg
577.50 USD 250µg
990.00 USD 500µg
1,650.00 USD 1mg
Looking for a custom size?
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Animal-Free Recombinant Human BMP-13/CDMP-2

BMP-13 is expressed in hypertrophic chondrocytes during embryonic development of long bones. Continued postnatal expression of BMP-13 in articular cartilage suggests that it plays a regulatory role in the growth and maintenance of articular cartilage. Adenovirus-mediated BMP-13 gene transfer to rabbit bone marrow stem cells have been reported to augment periosteal repair of osteochondral defects. The functional form of BMP-13/CDMP-2 is a disulfide-linked homodimer of two 120 amino-acid polypeptide chains. This 27.5 kDa protein is obtained by proteolytic processing of a biologically inactive precursor protein of 97.7kDa. Recombinant Human BMP-13/CDMP-2 is a 27.0 kDa homodimeric disulfide-linked protein consisting of two 120 amino acid polypeptide chains. 

Manufactured using all Animal-Free reagents.

Source: E.coli

Synonyms: Bone Morphogenetic Protein-13, GDF-6, Cartilage-Derived Morphogenetic Protein-2 (CDMP-2)

AA Sequence (monomer): TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR

Purity: ≥ 95% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to induce alkaline phosphatase production by ATDC-5 cells. The expected ED50 for this effect is 2.0-3.0 µg/ml.

New

Size

95.00 USD 10µg
215.00 USD 50µg
330.00 USD 100µg
577.50 USD 250µg
990.00 USD 500µg
1,650.00 USD 1mg
Looking for a custom size?
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Animal-Free Recombinant Human Enterokinase

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to, specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Enterokinase sequentially cleaves carboxyl side of D-D-D-D-K. Human Enterokinase is expressed as a linear 1019 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of Enterokinase, which consists of two polypeptide chains (heavy chain and light chain) held together by a single disulfide bond, resulting in formation of a biologically active heterodimer. The heavy chain consists of 784 amino acid residues, and the light chain consists of 235 amino acid residues. The calculated molecular weight of Recombinant Human Enterokinase is 108.7 kDa.

Manufactured using all Animal-Free reagents.

Source: CHO cells

Synonyms: None.

AA Sequence:

Heavy chain: LTIKESQRGA ALGQSHEARA TFKITSGVTY NPNLQDKLSV DFKVLAFDLQ QMIDEIFLSS NLKNEYKNSR VLQFENGSII VVFDLFFAQW VSDQNVKEEL IQGLEANKSS QLVTFHIDLN SVDILDKLTT TSHLATPGNV SIECLPGSSP CTDALTCIKA DLFCDGEVNC PDGSDEDNKM CATVCDGRFL LTGSSGSFQA THYPKPSETS VVCQWIIRVN QGLSIKLSFD DFNTYYTDIL DIYEGVGSSK ILRASIWETN PGTIRIFSNQ VTATFLIESD ESDYVGFNAT YTAFNSSELN NYEKINCNFE DGFCFWVQDL NDDNEWERIQ GSTFSPFTGP NFDHTFGNAS GFYISTPTGP GGRQERVGLL SLPLDPTLEP ACLSFWYHMY GENVHKLSIN ISNDQNMEKT VFQKEGNYGD NWNYGQVTLN ETVKFKVAFN AFKNKILSDI ALDDISLTYG ICNGSLYPEP TLVPTPPPEL PTDCGGPFEL WEPNTTFSST NFPNSYPNLA FCVWILNAQK GKNIQLHFQE FDLENINDVV EIRDGEEADS LLLAVYTGPG PVKDVFSTTN RMTVLLITND VLARGGFKAN FTTGYHLGIPEPCKADHFQC KNGECVPLVN LCDGHLHCED GSDEADCVRF FNGTTNNNGL VRFRIQSIWH TACAENWTTQ ISNDVCQLLG LGSGNSSKPI FSTDGGPFVK LNTAPDGHLI LTPSQQCLQD SLIRLQCNHK SCGKKLAAQD ITPK

Light Chain: IVGGSNAKEG AWPWVVGLYY GGRLLCGASL VSSDWLVSAA HCVYGRNLEP SKWTAILGLH MKSNLTSPQT VPRLIDEIVI NPHYNRRRKD NDIAMMHLEF KVNYTDYIQP ICLPEENQVF PPGRNCSIAG WGTVVYQGTT ANILQEADVP LLSNERCQQQ MPEYNITENM ICAGYEEGGI DSCQGDSGGP LMCQENNRWF LAGVTSFGYK CALPNRPGVY ARVSRFTEWI QSFLH

Purity: ≥ 90% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Sequentially cleaves carboxyl side of D-D-D-D-K.

New

Size

95.00 USD 5µg
215.00 USD 25µg
660.00 USD 100µg
1,155.00 USD 250µg
1,980.00 USD 500µg
3,300.00 USD 1mg
Looking for a custom size?
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Animal-Free Recombinant Human GRO-α/MGSA (CXCL1)

All three isoforms of GRO are CXC chemokines that can signal through the CXCR1 or CXCR2 receptors. The GRO proteins chemoattract and activate neutrophils and basophils. GRO/MGSA also stimulates mitogenesis in certain human melanoma cells. Recombinant Human GRO/MGSA is a 7.8 kDa protein consisting of 73 amino acids, including the 'ELR' motif common to the CXC chemokine family that binds to CXCR1 or CXCR2.

Manufactured using all Animal-Free reagents.

Source: E.coli

Synonyms: Growth Regulated Protein/Melanoma Growth Stimulatory Activity, MGSAα, NAP-3, GRO1

AA Sequence: ASVATELRCQ CLQTLQGIHP KNIQSVNVKS PGPHCAQTEV IATLKNGRKA CLNPASPIVK KIIEKMLNSD KSN

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Not available.

Note:

1mg will be provided as 2x500μg.

New

Size

95.00 USD 5µg
215.00 USD 20µg
396.00 USD 50µg
660.00 USD 100µg
1,155.00 USD 250µg
1,980.00 USD 500µg
3,300.00 USD 1mg
Looking for a custom size?
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Animal-Free Recombinant Human I-TAC (CXCL11)

I-TAC is a 'non-ELR' CXC chemokine that is regulated by interferon and signals through the CXCR3 receptor. I-TAC is chemoattractant for IL-2 activated T cells, but does not affect freshly isolated un-stimulated T cells, neutrophils, ormonocytes. Recombinant Human I-TAC (CXCL11) is an 8.3 kDa protein containing 73 amino acid residues, including the four highly conserved cysteine residues present in CXC chemokines. 

Manufactured using all Animal-Free reagents.

Source: E.coli

Synonyms: Interferon Inducible T-Cell α Chemokine, B-R1

AA Sequence: FPMFKRGRCL CIGPGVKAVK VADIEKASIM YPSNNCDKIE VIITLKENKG QRCLNPKSKQ ARLIIKKVER KNF

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to chemoattract human T-cells activated with IL-2.

New

Size

95.00 USD 5µg
215.00 USD 20µg
660.00 USD 100µg
1,155.00 USD 250µg
1,980.00 USD 500µg
3,300.00 USD 1mg
Looking for a custom size?
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Animal-Free Recombinant Human sTNF Receptor Type I

TNFRI belongs to the TNFR superfamily of transmembrane proteins, and is expressed in most cell types. Binding of either TNF-α or TNF-β to TNFRI initiates a signal transduction pathway that results in the activation of the transduction factor NF-κB, whose target genes are involved in the regulation of inflammatory responses, and, in certain cells induce apoptosis. Soluble TNF Receptor I (sTNFRI) is capable of inhibiting TNF-α and TNF-β activities by acting as a decoy receptor that serves as a sink for the TNF ligands. The human TNFRI gene encodes for a 455 amino acid type I transmembrane protein, which contains a 21 amino acid signal sequence, a 190 amino acid extracellular domain, a 23 amino acid transmembrane domain, and a 221 amino acid cytoplasmic domain. Recombinant Human sTNF Receptor Type I is an 18.3 kDa protein (162 amino acid residues) comprising the cysteine-rich, ligand-binding portion of the extracellular domain of the TNFRI protein.

Manufactured using all Animal-Free reagents.

Source: E.coli

Synonyms: soluble Tumor Necrosis Factor Type I, TNFRSF1A, TNFAR, p60, p55, CD120a, TNFR1

AA Sequence: MDSVCPQGKY IHPQNNSICC TKCHKGTYLY NDCPGPGQDT DCRECESGSF TASENHLRHC LSCSKCRKEM GQVEISSCTV DRDTVCGCRK NQYRHYWSEN LFQCFNCSLC LNGTVHLSCQ EKQNTVCTCH AGFFLRENEC VSCSNCKKSL ECTKLCLPQI EN

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its inhibitory effect of the TNF-α mediated cytotoxicity in murine L-929 cells. The  ED50  for this effect in the presence of 0.25 ng/ml of Recombinant Human TNF-α, is 0.05 µg/ml.

New

Size

95.00 USD 5µg
215.00 USD 20µg
660.00 USD 100µg
1,155.00 USD 250µg
1,980.00 USD 500µg
3,300.00 USD 1mg
Looking for a custom size?
Contact Us

Animal-Free Recombinant Human TECK (CCL25)

TECK is a CC chemokine, specifically expressed by thymic stromal cells, and signals through the CCR9 receptor. TECK is chemotactic towards activated macrophages, thymocytes and dendritic cells. Recombinant Human TECK is a 14.2 kDa protein containing 127 amino acid residues, including the four conserved cysteine residues present in CC chemokines.

Source: E.coli

Synonyms: Thymus Expressed Chemokine

AA Sequence: QGVFEDCCLA YHYPIGWAVL RRAWTYRIQE VSGSCNLPAA IFYLPKRHRK VCGNPKSREV QRAMKLLDAR NKVFAKLHHN MQTFQAGPHA VKKLSSGNSK LSSSKFSNPI SSSKRNVSLL ISANSGL

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Not available.

New

Size

95.00 USD 5µg
215.00 USD 20µg
396.00 USD 50µg
660.00 USD 100µg
1,155.00 USD 250µg
1,980.00 USD 500µg
3,300.00 USD 1mg
Looking for a custom size?
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Animal-Free Recombinant Murine BD-3

Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors, and are released by proteolytic cleavage of a signal sequence and, in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant Murine BD-3 is a 4.6 kDa protein containing 41 amino acid residues.

Manufactured using all Animal-Free reagents.

Source: E.coli

Synonyms: Beta-Defensin 3, DEFB3, DEFB103A

AA Sequence: KKINNPVSCL RKGGRCWNRC IGNTRQIGSC GVPFLKCCKR K

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Not available.

New

Size

95.00 USD 2µg
215.00 USD 10µg
1,140.00 USD 100µg
1,995.00 USD 250µg
3,420.00 USD 500µg
5,700.00 USD 1mg
Looking for a custom size?
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Animal-Free Recombinant Murine IL-21

IL-21 is a pleiotropic cytokine produced by CD4+ T cells in response to antigenic stimulation. Its action generally enhances antigen-specific responses of immune cells. The biological effects of IL-21 include: inducing the differentiation of T-cell-stimulated B-cells into plasma cells and memory B-cells; the stimulation of IgG production in conjunction with IL-4; and the induction of apoptotic effects in naïve B-cells and stimulated B-cells in the absence of T-cell signaling. Additionally, IL-21 promotes the anti-tumor activity of CD8+ T-cells and NK cells. IL-21 exerts its effect through binding to a specific type I cytokine receptor, IL-21R, which also contains the γ chain (γc) found in other cytokine receptors, including IL-2, IL-4, IL-7, IL-9 and IL-15. The IL-21/IL-21R interaction triggers a cascade of events, which includes activation of the tyrosine kinases JAK1 and JAK3, followed by activation of the transcription factors STAT1 and STAT3. Recombinant Murine IL-21 is a 15.0 kDa protein consisting of 130 amino acid residues.

Manufactured using all Animal-Free reagents.

Source: E.coli

Synonyms: Interleukin-21, Za11

AA Sequence: MHKSSPQGPD RLLIRLRHLI DIVEQLKIYE NDLDPELLSA PQDVKGHCEH AAFACFQKAK LKPSNPGNNK TFIIDLVAQL RRRLPARRGG KKQKHIAKCP SCDSYEKRTP KEFLERLKWL LQKMIHQHLS

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to stimulate the proliferation of human ANBL-6 cells. The expected ED50 is ≤ 1.0 ng/ml, corresponding to a specific activity of ≥ 1 x 106 units/mg.

New

Size

275.00 USD 500mL
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PeproGrow™ hMSC Mesenchymal Stem Cell Media

PeproGrow hMSC (Mesenchymal Stem Cell) Medium is a xeno-free, human serum containing, phenol red-free complete media formulation originally designed for thein vitro expansion of adipose-derived human mesenchymal stem cells (ADMSCs) while maintaining full multipotency. Since its design, this media formulation has been shown to be suitable for the sustained growth of adipose tissue-derived, bone marrow-derived, umbilical cord-derived, placental-derived, and urine-derived MSCs in both adherent and suspension culture. For optimal results, culturing should be conducted on a surface coated with PeproTech’s Animal-Free Human Vitronectin Matrix as a surface-coating reagent; however, other suitable extracellular matrix (ECM) proteins, such as fibronectin or vitronectin, can be used. PeproGrow hMSC Medium was designed and developed in collaboration with American CryoStem Corporation, and is supplied as a 500mL bottle of PeproGrow hMSC Basal Medium containing a human serum component, and a separate, lyophilized vial of animal-free PeproGrow hMSC Growth Factor Supplement. The addition of the separate, lyophilized growth factor supplement to the basal medium results in a complete medium containing all growth factors and supplements necessary for optimal expansion of human mesenchymal stem cells in culture. Additional companion products, including PeproTech’s Animal-Free Vitronectin Matrix and Buffer Kit, are available separately.

MSC growth curve

 

New

Size

80.00 USD 5µg
195.00 USD 25µg
750.00 USD 100µg
1,365.00 USD 250µg
2,340.00 USD 500µg
3,900.00 USD 1mg
Looking for a custom size?
Contact Us

Recombinant Human FGF-BP-1

The Fibroblast Growth Factor (FGF) Superfamily is comprised of multifunctional proteins that serves to regulate several complex biological processes related to the development, restoration, and/or redistribution of prenatal and postnatal tissue, as well as angiogenesis, wound healing, nerve regeneration, chronic inflammation, and cancer growth. Members of the FGF Superfamily function through paracrine, autocrine and intracrine pathways to promote spatial and temporal integrations of several cell responses, such as proliferation, growth, differentiation, and migration. Fibroblast growth factor binding protein 1 (FGF-BP-1) is a secreted glycoprotein, which contains both a heparin-binding domain and a distinct FGF-binding region, that is shed into circulation where it acts as a chaperone molecule for FGFs, most notably FGF-acidic and FGF-basic. Once secreted, FGF-BP-1 can bind FGFs in a reversible manner to mobilize them from inactive storage on heparan sulfate proteoglycans in the extracellular matrix, and deliver them to high affinity receptors on the cell surface where they can exert biological function, all the while protecting against proteolytic degradation. Expressed within the squamous epithelium, FGF-BP-1 functions synergistically with FGFs as a mitogen for keratinocytes and an antagonist for angiogenesis under normal physiological conditions and instances of tissue repair, while also acting as an angiogenic switch for the malignant progression of epithelial cells. First discovered at elevated levels within A431 human epidermoid carcinoma cells, FGF-BP-1 is also expressed at elevated levels in many squamous cell carcinomas and tumors where it has been shown to be a rate-determining factor, interacting with the heparan sulfate proteoglycan perlecan to potentiate neovascularization of tumor masses. Recombinant Human FGF-BP-1 expressed in E.coli is a 24.0 kDa protein containing 212 amino acid residues.

Source: E.coli

Synonyms: Fibroblast growth factor binding protein 1, FGF-BP, FGF-binding protein 1, HBp17

AA Sequence: MKKKVKNGLH SKVVSEQKDT LGNTQIKQKS RPGNKGKFVT KDQANCRWAA TEQEEGISLK VECTQLDHEF SCVFAGNPTS CLKLKDERVY WKQVARNLRS QKDICRYSKT AVKTRVCRKD FPESSLKLVS STLFGNTKPR KEKTEMSPRE HIKGKETTPS SLAVTQTMAT KAPECVEDPD MANQRKTALE FCGETWSSLC TFFLSIVQDT SC

Purity: ≥ 95% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF receptors. The expected ED50 for this effect is 1.5-3.0 μg/ml.

New

Size

80.00 USD 10µg
195.00 USD 50µg
300.00 USD 100µg
525.00 USD 250µg
900.00 USD 500µg
1,500.00 USD 1mg
Looking for a custom size?
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Recombinant Human ICOS Fc

Inducible T-cell costimulator (ICOS) is a T-cell-specific, surface receptor of the immunoglobulin superfamily that binds inducible costimulatory ligand (ICOSL), alternatively referred to as B7-H2, to play a critical role in the development and function of regulatory T-cells (Tregs). ICOS joins CD28, CTLA-4 and PD-1 as a member of the growing CD28/CTLA-4 family of costimulatory immunoreceptors that function synergistically with members of the B7 family of transmembrane ligands, including B7-1, B7-2, B7-H1 (PD-L1), B7-H2 and PD-L2, to constitute crucial costimulatory pathways for T-cell and B-cell regulatory responses. As the main receptor of B7-H2, ICOS can have both negative and positive influence over immune response, including the direct downregulation of B7-H2, and is critically involved in the immunosuppression of tumor-associated memory CD4+ T-cells. Interaction between ICOS and B7-H2 on the surface of antigen presenting cells potentiates costimulatory signals responsible for enhancing basic T-cell response to foreign antigens, namely the augmentation of T-cell proliferation, the upregulation of molecules responsible for mediating intercellular interaction, and the secretion of cytokines such as IL-4, IL-10 and IL-21. The significant involvement of ICOS and B7-H2 interaction within an array of immunological responses, such as those of Th1, Th2 and Th17 cells, means that the blockade of this interaction has been linked to a number of autoimmune diseases, including rheumatoid arthritis (RA), inflammatory bowel disease (IBD), type 1 diabetes, and graft versus host disease (GVHD). Unlike CD28, which is constitutively expressed on the surface of T-cells where it has restricted interaction with B7-H2, ICOS is expressed at low levels on naive T-cells and is upregulated on activated T-cells and regulatory T-cells (Tregs) after TCR ligation and CD28 stimulation. PeproTech's CHO cell-derived Recombinant Human ICOS Fc is a glycosylated, homodimer 79.4 kDa of 706 amino acid residues whose monomer consists of the 120-amino-acid-length extracellular portion of ICOS fused to the 231-amino-acid-length Fc portion of human IgG1 by two glycines. The calculated molecular weight of Recombinant Human ICOS Fc dimer is 79.4 kDa; however, due to glycosylation, it migrates at an apparent molecular weight of approximately 40-45 kDa by SDS-PAGE analysis under reducing conditions.

Source: CHO cells

Synonyms: Inducible T-cell costimulator, CD278, Activation-inducible lymphocyte immunomediatory molecule (AILIM), CRP-1, CVID1

AA Sequence (monomer): EINGSANYEM FIFHNGGVQI LCKYPDIVQQ FKMQLLKGGQ ILCDLTKTKG SGNTVSIKSL KFCHSQLSNN SVSFFLYNLD HSHANYYFCN LSIFDPPPFK VTLTGGYLHI YESQLCCQLK GGPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK

Purity: ≥ 95% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to cause adhesion of the human HL-60 monocytic cells in the presence of 2% PHA.

New

Size

80.00 USD 2µg
195.00 USD 10µg
1,040.00 USD 100µg
1,820.00 USD 250µg
3,120.00 USD 500µg
5,200.00 USD 1mg
Looking for a custom size?
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Recombinant Human IL-36α (IL-1F6)

The IL-1 family is comprised of 11 structurally related ligands, including recently re-named IL-36α (IL-1F6), β (IL-1F8), and γ (IL-1F9). IL-36α is highly expressed in psoriatic plaques, as are IL-36β and IL-36γ, and is the only IL-1 family member found to be expressed by T-cells, as well as monocytes and B-cells. Primarily found in skin and lymphoid tissues, IL-36α is also found to a lesser extent in tissues of the fetal brain, trachea, stomach, and intestine. IL-36α signals through a combination of the IL-1Rrp2 (IL-1R6) receptor, which is primarily expressed on certain dendritic cells, and the widely expressed IL-RAcP (IL-1 receptor accessory protein). IL-36α also functions as an agonist of NF-kappaB and MAPK pathways, and induces the production of proinflammatory cytokines and chemokines, including IL-6, IL-8, BD-2, and BD-3. Recombinant human IL-36α is a 17.2 kDa protein containing 154 amino acid residues.

Source: E.coli

Synonyms: Interleukin-36α, IL36A, Interleukin-1 family member 6 (IL-1F6), FIL1ε (FIL1E), Interleukin-1ε (IL1E)

AA Sequence: MKIDTPQQGS IQDINHRVWV LQDQTLIAVP RKDRMSPVTI ALISCRHVET LEKDRGNPIY LGLNGLNLCL MCAKVGDQPT LQLKEKDIMD LYNQPEPVKS FLFYHSQSGR NSTFESVAFP GWFIAVSSEG GCPLILTQEL GKANTTDFGL TMLF

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Measured by its ability to inhibit secretion of IL-8 by A431 cells in the prescence of IL-36γ.

New

Size

80.00 USD 20µg
195.00 USD 100µg
385.00 USD 250µg
660.00 USD 500µg
1,100.00 USD 1mg
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Recombinant Human PD-L2 Fc

Programmed death-ligand 2 (PD-L2), or B7-DC, is a member of the B7 ligand family within the immunoglobulin superfamily that, along with programmed death-ligand 1 (PD-L1), acts as a ligand for programmed cell death protein 1 (PD-1). Though expressed primarily in dendritic cells, PD-L2 expression can be induced on a wide variety of immune and non-immune cells depending on the microenvironment. PD-L2 expression is particularly upregulated in the presence of Th2 cytokine, IL-4, as well as Th1 cytokines, TNF-α and IFN-γ to a lesser degree. While generally expressed at lower levels compared to PD-L1, PD-L2 demonstrates a 2 to 6 times higher relative affinity to PD-1 than PD-L1. PD-1 and its ligands are referred to as inhibitory immune checkpoint molecules in that they provide useful negative feedback during physiological homeostasis. Ligation of PD-L2 or PD-L1 inhibits activation, proliferation, and cytokine secretion (e.g. IFN-gamma, IL-10) in T cells, ultimately dampening immune response. Conversely, studies have shown that PD-L2 can also stimulate T-cell proliferation and cytokine production, even in PD-1-deficient T cells, suggesting additional receptors. Recent studies have concluded that PD-L2 also binds to a second receptor, repulsive guidance molecule b (RGMb), which was originally identified as a receptor for bone morphogenetic proteins (BMPs). RGMb is expressed in the central nervous system, as well as in macrophages, however, its role in immunity is only beginning to emerge. Interaction between PD-L2 and RGMb regulates the development of respiratory tolerance in the lung through BMP and/or neogenin signaling pathways. The naturally occurring human PD-L2 monomer consists of a 201-amino-acid extracellular domain, a 21-amino-acid transmembrane domain, and a 32-amino-acid cytoplasmic domain. PeproTech’s CHO cell-derived Recombinant Human PD-L2 Fc is a glycosylated, disulfide-linked homodimer of 433-amino-acid residues whose monomer consists of a 200-amino-acid portion of mature PD-L2, including Leu20 through Pro219, fused to the 231-amino-acid length Fc portion of human IgG1 by two glycines. The calculated molecular weight of monomeric CHO cell-derived Recombinant Human PD-L2 Fc is 48.6 kDa; however, due to glycosylation, it migrates at an apparent molecular weight of approximately 65-75 kDa by SDS-PAGE analysis under reducing conditions.

Source: CHO cells

Synonyms: Programmed cell death 1 ligand 2 (PDCD1 ligand 2), PD-1 ligand 2, Programmed death ligand 2, Butyrophilin B7-DC, CD273, PDCD1LG2, PDCD1L2, PDLB7DC

AA Sequence (monomer): LFTVTVPKEL YIIEHGSNVT LECNFDTGSH VNLGAITASL QKVENDTSPH RERATLLEEQ LPLGKASFHI PQVQVRDEGQ YQCIIIYGVA WDYKYLTLKV KASYRKINTH ILKVPETDEV ELTCQATGYP LAEVSWPNVS VPANTSHSRT PEGLYQVTSV LRLKPPPGRN FSCVFWNTHV RELTLASIDL QSQMEPRTHP GGPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGK

Purity: ≥ 95% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to bind programmed cell death ligand 1 (PD-1) in a functional ELISA.

New

Size

80.00 USD 5µg
195.00 USD 20µg
780.00 USD 100µg
1,365.00 USD 250µg
2,340.00 USD 500µg
3,900.00 USD 1mg
Looking for a custom size?
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Recombinant Human Sclerostin

Sclerostin, a glycoprotein predominantly secreted by osteocytes, is a member of the Cerberus/DAN family of putative BMP antagonists that functions as an endogenous regulator of the canonical Wnt signaling pathway and an inhibitory regulator of bone homeostasis. Although expressed nearly exclusively by osteocytes, sclerostin can also be found at significant levels elsewhere, such as bone, bone marrow, cartilage, the kidney, and the liver, and has also been shown to be produced by hypertrophic chondrocytes and cementocytes. Like DKK family members DKK-1 and DKK-4, sclerostin plays an important regulatory role in the Wnt/β-catenin signaling pathway by forming inhibitory complexes with LDL Receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/β-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/β-catenin signaling cascade. Sclerostin has also been shown to interact directly with LRP4 via its extracellular domain to facilitate inhibition of Wnt signaling, and can catabolically promote osteoclast activity by increasing osteocyte expression of RANKL. Sclerostin’s critical involvement in the regulation of bone formation and resorption is emphasized by two bone dysplasia disorders, sclerosteosis and van Buchem disease (VBD), caused by rare autosomal recessive mutations that result in progressive bone overgrowth and hypermineralization due to markedly decreased sclerostin levels. PeproTech's CHO cell-derived Recombinant Human Sclerostin is a 186-amino-acid-length glycoprotein with a calculated molecular weight of 21.0 kDa. As a result of glycosylation, Recombinant Human Sclerostin migrates with an apparent molecular mass of approximately 26-32 kDa by SDS-PAGE gel, under non-reducing conditions.

Source: CHO cells

Synonyms: SOST, SOST1, CDD, VBCH, DAND6

AA Sequence: AFKNDATEII PELGEYPEPP PELENNKTMN RAENGGRPPH HPFETKDVSE YSCRELHFTR YVTDGPCRSA KPVTELVCSG QCGPARLLPN AIGRGKWWRP SGPDFRCIPD RYRAQRVQLL CPGGEAPRAR KVRLVASCKC KRLTRFHNQS ELKDFGTEAA RPQKGRKPRP RARSAKANQA ELENAY

Purity: ≥ 95% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to downregulate alkaline phosphatase activity in differentiating MC3T3‑E1 cells in the presence of 20ng/ml murine Wnt‑3a.

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Recombinant Human Semaphorin 3A Fc

Semaphorins are a large group of structurally-related, secreted, GPI-anchored, transmembrane, cell-signaling molecules. There are 8 major classifications of Semaphorins (the first seven ordered by number, 1-7, and the eighth designated V for virus), which are characterized by the existence of a conserved 500 amino acid SEMA domain at the amino terminus. Classes 3, 4, 6, and 7 are found in vertebrates only, whilst class 5 is found in both vertebrates and invertebrates. Each class is then divided into additional subgroups based on shared structural characteristics.  Semaphorins primarily function as axon growth cone guidance factors during neuronal development. Semaphorin 3A acts as a chemo-repellent to axons, and an inhibitor of the growth of axons by signaling through receptors, Neuropilin-1 and Plexin-A.  PeproTech's CHO cell-derived Recombinant Human Semaphorin 3A Fc is a glycosylated, disulfide-linked homodimer of 1,976 amino acid residues, which includes the SEMA domain, immunoglobulin c2-like domain, and the C-terminal basic Arg/Lys-rich domain of the mature sequence, as well as an 8-residue N-terminal His-tag and a 230-residue C-terminal Fc region linked by two glycines. Recombinant Human Semaphorin 3A Fc has a calculated molecular weight of 226.2 kDa and therefore runs above the 200kDa marker by SDS-PAGE analysis under nonreducing conditions. When run under reducing conditions, this protein migrates as three distinct bands that, due to glycosylation, run higher than expected at apparent molecular weights of approximately 120-130 kDa, 90-100 kDa, and 35-40 kDa.

Source: CHO cells

Synonyms: SEMA3A, SEMAD

AA Sequence (monomer): HHHHHHHHGK NNVPRLKLSY KEMLESNNVI TFNGLANSSS YHTFLLDEER SRLYVGAKDH IFSFDLVNIK DFQKIVWPVS YTRRDECKWA GKDILKECAN FIKVLKAYNQ THLYACGTGA FHPICTYIEI GHHPEDNIFK LENSHFENGR GKSPYDPKLL TASLLIDGEL YSGTAADFMG RDFAIFRTLG HHHPIRTEQH DSRWLNDPKF ISAHLISESD NPEDDKVYFF FRENAIDGEH SGKATHARIG QICKNDFGGH RSLVNKWTTF LKARLICSVP GPNGIDTHFD ELQDVFLMNF KDPKNPVVYG VFTTSSNIFK GSAVCMYSMS DVRRVFLGPY AHRDGPNYQW VPYQGRVPYP RPGTCPSKTF GGFDSTKDLP DDVITFARSH PAMYNPVFPM NNRPIVIKTD VNYQFTQIVV DRVDAEDGQY DVMFIGTDVG TVLKVVSIPK ETWYDLEEVL LEEMTVFREP TAISAMELST KQQQLYIGST AGVAQLPLHR CDIYGKACAE CCLARDPYCA WDGSACSRYF PTAKRATRAQ DIRNGDPLTH CSDLHHDNHH GHSPEERIIY GVENSSTFLE CSPKSQRALV YWQFQRRNEE RKEEIRVDDH IIRTDQGLLL RSLQQKDSGN YLCHAVEHGF IQTLLKVTLE VIDTEHLEEL LHKDDDGDGS KTKEMSNSMT PSQKVWYRDF MQLINHPNLN TMDEFCEQVW KRDRKQRRQR PGHTPGNSNK WKHLQENKKG RNRRTHEFER APRSVGGPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGK

Purity: ≥ 95% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to bind recombinant rat Neuropilin‐1 Fc Chimera in a functional ELISA assay.

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Recombinant Human TLR-4

Characterized by N-terminal domains rich in leucine repeats and C-terminal intracellular Toll/interleukin (IL)-1 (TIL) domains, the structurally-related members of the Toll-like Receptor (TLR) family are abundantly expressed, transmembrane signaling receptors that play integral roles in the induction of innate and adaptive immunity. As members of the larger family of pattern recognition receptors, TLRs recognize and respond to pathogen-associated molecular patterns (PAMPs) and endogenous damage-associated molecular patterns (DAMPs) by initiating activation of NF-κB and the release of inflammatory mediators. Constitutively expressed in cells of the immune system, TLR-4 is secreted at significantly amplified levels in response to high concentrations of LPS, the major cell wall component of gram-negative bacteria that acts as the key ligand for TLR-4 inflammatory response. TLR-4 mounts a defense against infection through an intricate process involving interaction with co-stimulatory molecules, such as myeloid differentiation factor 88 (MyD88), NF-κB, LPS-Binding Protein (LBP), CD14, and MD-2, and the instigation of intracellular signaling cascade that prompts the NF-κB, Wnt/β-catenin, and mitogen-activated protein kinase (MAPK) pathways to secrete proinflammatory cytokines and chemokines. Myeloid differentiation protein-2 (MD-2), also referred to as LY96, is essential to TLR-4-mediated response to LPS due to its binding of both the extracellular domain of TLR-4, which serves to localize TLR-4 on the cell surface, and LPS to form the TLR-4/MD-2/LPS complex, which can be used for the in vitro removal of endotoxin from biological samples. The activation of TLR-4/MD-2 begins with the detection of LPS by circulating LBP, which in turn facilitates an association between LPS and CD14 for the formation of a CD14-LPS complex that transports and presents LPS to the TLR-4/MD-2 signaling complex, and culminates in the activation of downstream signaling events. Inflammatory response can also be triggered by the formation of a heterodimeric complex between TLR-6 and TLR-4, the internalization of which results in NF-κB-dependent secretion of CXCL1, as well as the production of proinflammatory cytokines, such as IL-1β, and the production of inflammatory regulating chemokines, such as CXCL2, CCL5 and CCL9. Considering TLR-4’s connections to immunity, inflammatory response, proliferation, apoptosis and angiogenesis, it is no surprise that irregular expression of TLR-4 has been linked to various malignant cell types, a number of autoimmune conditions genetically linked to psoriasis, and a number of other diseases. Recombinant Human TLR-4 is a 69.3 kDa glycoprotein containing 609 amino acid residues of the TLR-4 extracellular domain. As a result of glycosylation, Recombinant Human TLR-4 migrates with an apparent molecular mass of approximately 90-100 kDa by SDS-PAGE gel, under reducing and non-reducing conditions.

Source: HEK293 cells

Synonyms: Toll-like receptor 4, TOLL, CD284, ARMD10

AA Sequence: ESWEPCVEVV PNITYQCMEL NFYKIPDNLP FSTKNLDLSF NPLRHLGSYS FFSFPELQVL DLSRCEIQTI EDGAYQSLSH LSTLILTGNP IQSLALGAFS GLSSLQKLVA VETNLASLEN FPIGHLKTLK ELNVAHNLIQ SFKLPEYFSN LTNLEHLDLS SNKIQSIYCT DLRVLHQMPL LNLSLDLSLN PMNFIQPGAF KEIRLHKLTL RNNFDSLNVM KTCIQGLAGL EVHRLVLGEF RNEGNLEKFD KSALEGLCNL TIEEFRLAYL DYYLDDIIDL FNCLTNVSSF SLVSVTIERV KDFSYNFGWQ HLELVNCKFG QFPTLKLKSL KRLTFTSNKG GNAFSEVDLP SLEFLDLSRN GLSFKGCCSQ SDFGTTSLKY LDLSFNGVIT MSSNFLGLEQ LEHLDFQHSN LKQMSEFSVF LSLRNLIYLD ISHTHTRVAF NGIFNGLSSL EVLKMAGNSF QENFLPDIFT ELRNLTFLDL SQCQLEQLSP TAFNSLSSLQ VLNMSHNNFF SLDTFPYKCL NSLQVLDYSL NHIMTSKKQE LQHFPSSLAF LNLTQNDFAC TCEHQSFLQW IKDQRQLLVE VERMECATPS DKQGMPVLSL NITCQMNKT

Purity: ≥ 95% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to bind rhMD-2 in a functional ELISA.

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Recombinant Murine IL-36RA

The IL-1 family is comprised of 11 structurally related ligands, including the recently re-named IL-36RA (IL-1F5), IL-36α (IL-1F6), IL-36β (IL-1F8), and IL-36γ (IL-1F9). The interaction of IL-36 ligands with the IL-1Rrp2 receptor (IL-1R6) can induce various activities, including dendritic cell maturation and activation. IL-36RA can antagonize the NF-κB signaling induced by either IL-36α, β or γ by binding to the IL-1Rrp2 receptor in a manner that prevents the initiation of functional signaling. Recombinant Murine IL-36RA is an E.coli-derived 16.9 kDa protein containing 154 amino acid residues.

Source: E.coli

Synonyms: Interleukin-36RA, FIL1 delta, IL-1F5, IL-1HY1, IL-1L1, IL-1RP3, IL-1ra Homolog 1, IL-1 delta

AA Sequence: VLSGALCFRM KDSALKVLYL HNNQLLAGGL HAEKVIKGEE ISVVPNRALD ASLSPVILGV QGGSQCLSCG TEKGPILKLE PVNIMELYLG AKESKSFTFY RRDMGLTSSF ESAAYPGWFL CTSPEADQPV RLTQIPEDPA WDAPITDFYF QQCD

Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Measured by its ability to inhibit secretion of IL-8 by A431 cells in the presence of human IL-36γ.

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Anti-Human Amphiregulin

Source: Polyclonal Rabbit

Preparation: Produced from sera of rabbits immunized with highly pure Recombinant Human Amphiregulin. Anti-Human Amphiregulin-specific antibody was purified by affinity chromatography employing an immobilized Human Amphiregulin matrix.

Immunogen: E.coli derived Recombinant Human Amphiregulin (PeproTech catalog# 100-55B)

Sandwich ELISA: To detect Human Amphiregulin by sandwich ELISA (using 100μl/well), a concentration of 0.5-2.0 μg/ml of this antibody is required. This antigen affinity purified antibody, in conjunction with PeproTech’s Biotinylated Anti-Human Amphiregulin (500-P322Bt) as a detection antibody, allows the detection of at least 2000-4000 pg/ml of Recombinant Human Amphiregulin.

Anti-Human Amphiregulin Sandwich ELISA

Western Blot: To detect Human Amphiregulin by Western Blot analysis this antibody can be used at a concentration of 0.1-0.2 μg/ml. When used in conjunction with compatible secondary reagents, the detection limit for Recombinant Human Amphiregulin is 1.5-3.0 ng/lane, under either reducing or non-reducing conditions.

Anti-Human Amphiregulin Western Blot Unreduced Anti-Human Amphiregulin Western Blot Reduced

Note:

Additional applications tested on a lot-to-lot basis. Please contact Technical Support for more information.

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Anti-Human BAFF (Polyclonal Rabbit)

Source: Polyclonal Rabbit

Preparation: Produced from sera of rabbits immunized with highly pure Recombinant Human BAFF. Anti-Human BAFF-specific antibody was purified by affinity chromatography employing an immobilized Human BAFF matrix.

Immunogen: E.coli derived Recombinant Human BAFF (PeproTech catalog# 310-13)

Sandwich ELISA: To detect Human BAFF by sandwich ELISA (using 100μl/well) a concentration of 0.5-2.0 μg/ml of this antibody is required. This antigen affinity purified antibody, in conjunction with PeproTech’s Biotinylated Anti-Human BAFF (500-P163BT) as a detection antibody, allows the detection of at least 2000-4000 pg/ml of Recombinant Human BAFF.

Anti-Human BAFF Sandwich ELISA

Western Blot: To detect Human BAFF by Western Blot analysis this antibody can be used at a concentration of 0.1-0.2 μg/ml. When used in conjunction with compatible secondary reagents the detection limit for Recombinant Human BAFF is 1.5-3.0 ng/lane, under either reducing or non-reducing conditions.

Anti-Human BAFF Western Blot Unreduced Anti-Human BAFF Western Blot Reduced

Note:

Additional applications tested on a lot‐to‐lot basis. Please contact Technical Support for more information.

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