RUO Cytokines

Other Proteins

Products listed here include polypeptides that do not fit into any of the other protein categories. This list of products includes peptides, proteins that act primarily as structural proteins, protease inhibitors, non-protease enzymes, intracellular regulatory proteins, and proteins that perform various other functions.

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195.00 USD 100µg
385.00 USD 250µg
660.00 USD 500µg
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Recombinant Human ApoA-I

ApoA-I is a 29.0 kDa protein produced in the liver and intestine, and secreted as the predominant constituent of nascent high density lipoprotein (HDL) particle.  ApoA-I, which is found exclusively in HDL, has a unique ability to capture and solubilize free cholesterol.  This ApoA-I ability enables HDL to remove excess peripheral cholesterol, and return it to the liver for recycling and excretion.  This process, called reverse cholesterol transport, is thought to inhibit atherogenesis.  For this reason, HDL is also known as the “good cholesterol.”  The therapeutic potential of ApoA-I has been recently assessed in patients with acute coronary syndromes, using a recombinant form of a naturally occurring variant of ApoA-I (called ApoA-I Milano).  The availability of recombinant normal ApoA-I should facilitate further investigation into the potential usefulness of ApoA-I in preventing atherosclerotic vascular diseases.  Recombinant Human ApoA-I is a 28.2 kDa protein of 244 amino acid residues.

Source: E.coli

Synonyms: Apolipoprotein A-I

AA Sequence: MDEPPQSPWD RVKDLATVYV DVLKDSGRDY VSQFEGSALG KQLNLKLLDN WDSVTSTFSK LREQLGPVTQ EFWDNLEKET EGLRQEMSKD LEEVKAKVQP YLDDFQKKWQ EEMELYRQKV EPLRAELQEG ARQKLHELQE KLSPLGEEMR DRARAHVDAL RTHLAPYSDE LRQRLAARLE ALKENGGARL AEYHAKATEH LSTLSEKAKP ALEDLRQGLL PVLESFKVSF LSALEEYTKK LNTQ

Purity: Greater than 97% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Not available.

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195.00 USD 500µg
350.00 USD 1mg
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Recombinant Human ApoE2

ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism.  In addition to facilitating solubilization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism.  Significant quantities of ApoE are produced in the liver and brain, and to some extent in almost every organ.  ApoE is an important constituent of all plasma lipoproteins.  Its interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism.  It also binds with the LDL receptor (apo B/E).  Defects in ApoE are a cause of hyperlipoproteinemia type III.  ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution.  Compared with E3 and E4, E2 exhibits the lowest receptor binding affinity.  E2 allele carriers had significantly lower levels of total cholesterol, low-density lipoprotein cholesterol, and non-high-density lipoprotein cholesterol, as well as increased ApoE levels.  Recombinant Human ApoE2 is a 34.3 kDa protein containing 300 amino acid residues.

Source: E.coli

Synonyms: Apolipoprotein E2

AA Sequence: MKVEQAVETE PEPELRQQTE WQSGQRWELA LGRFWDYLRW VQTLSEQVQE ELLSSQVTQE LRALMDETMK ELKAYKSELE EQLTPVAEET RARLSKELQA AQARLGADME DVCGRLVQYR GEVQAMLGQS TEELRVRLAS HLRKLRKRLL RDADDLQKCL AVYQAGAREG AERGLSAIRE RLGPLVEQGR VRAATVGSLA GQPLQERAQA WGERLRARME EMGSRTRDRL DEVKEQVAEV RAKLEEQAQQ IRLQAEAFQA RLKSWFEPLV EDMQRQWAGL VEKVQAAVGT SAAPVPSDNH

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

Biological Activity: Not available.

Note:

1mg will be provided as 2x500μg.

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195.00 USD 500µg
350.00 USD 1mg
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Recombinant Human ApoE3

ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism.  In addition to facilitating solubilization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism.  Significant quantities of ApoE are produced in the liver and brain, and to some extent in almost every organ.  ApoE is an important constituent of all plasma lipoproteins.  Its interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism.  It also binds with the LDL receptor (apo B/E).  Defects in ApoE are a cause of hyperlipoproteinemia type III.  ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution.  E3 is the most common isoform and is present in 40-90% of the population.  Recombinant Human ApoE3 is a 34.0 kDa protein containing 300 amino acid residues.

Source: E.coli

Synonyms: Apoprotein E3

AA Sequence: MKVEQAVETE PEPELRQQTE WQSGQRWELA LGRFWDYLRW VQTLSEQVQE ELLSSQVTQE LRALMDETMK ELKAYKSELE EQLTPVAEET RARLSKELQA AQARLGADME DVCGRLVQYR GEVQAMLGQS TEELRVRLAS HLRKLRKRLL RDADDLQKRL AVYQAGAREG AERGLSAIRE RLGPLVEQGR VRAATVGSLA GQPLQERAQA WGERLRARME EMGSRTRDRL DEVKEQVAEV RAKLEEQAQQ IRLQAEAFQA RLKSWFEPLV EDMQRQWAGL VEKVQAAVGT SAAPVPSDNH

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

Biological Activity: Not available.

Note:

1mg will be provided as 2x500μg.

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195.00 USD 500µg
350.00 USD 1mg
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Recombinant Human ApoE4

ApoE belongs to a group of proteins that bind reversibly with lipoprotein and play an important role in lipid metabolism.  In addition to facilitating solubilization of lipids, these proteins help to maintain the structural integrity of lipoproteins, serve as ligands for lipoprotein receptors, and regulate the activity of enzymes involved in lipid metabolism.  Significant quantities of ApoE are produced in the liver and brain, and to some extent in almost every organ.  ApoE is an important constituent of all plasma lipoproteins.  Its interaction with specific ApoE receptor enables uptake of chylomicron remnants by liver cells, which is an essential step during normal lipid metabolism.  It also binds with the LDL receptor (apo B/E).  Defects in ApoE are a cause of hyperlipoproteinemia type III.  ApoE exists in three major isoforms; E2, E3, and E4, which differ from one another by a single amino-acid substitution.  Individuals heterozygous for the ApoE4 allele are at higher risk of late-onset Alzheimer’s disease.  Recombinant Human ApoE4 is a 34.4 kDa protein containing 300 amino acid residues.

Source: E.coli

Synonyms: Apolipoprotein E4

AA Sequence: MKVEQAVETE PEPELRQQTE WQSGQRWELA LGRFWDYLRW VQTLSEQVQE ELLSSQVTQE LRALMDETMK ELKAYKSELE EQLTPVAEET RARLSKELQA AQARLGADME DVRGRLVQYR GEVQAMLGQS TEELRVRLAS HLRKLRKRLL RDADDLQKRL AVYQAGAREG AERGLSAIRE RLGPLVEQGR VRAATVGSLA GQPLQERAQA WGERLRARME EMGSRTRDRL DEVKEQVAEV RAKLEEQAQQ IRLQAEAFQA RLKSWFEPLV EDMQRQWAGL VEKVQAAVGT SAAPVPSDNH

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

Biological Activity: Not available.

Note:

1mg will be provided as 2x500μg.

Size
80.00 USD 10µg
195.00 USD 50µg
215.00 USD 100µg
280.00 USD 250µg
480.00 USD 500µg
800.00 USD 1mg
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Recombinant Human Apo-SAA

Human Apo-SAA is a 104 amino acid polypeptide that circulates primarily 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 polypeptide, which contains an 18 amino acid N-terminal signal sequence. Recombinant Apo-SAA is a consensus SAA molecule corresponding to human Apo-SAA1α, except for the presence of an N-terminal methionine, the substitution of asparagine for aspartic acid at position 60, and arginine for histidine at position 71 (the latter two substituted residues are present in Apo-SAA2β).  The calculated molecular weight of Recombinant Human Apo-SAA is 11.7 kDa.

Source: E.coli

Synonyms: None

AA Sequence: MRSFFSFLGE AFDGARDMWR AYSDMREANY IGSDKYFHAR GNYDAAKRGP GGVWAAEAIS NARENIQRFF GRGAEDSLAD QAANEWGRSG KDPNHFRPAG LPEKY

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

Biological Activity: Tested by its ability to down-regulate lipid biosynthesis in aortic smooth muscle cells. The effective concentration was found to be 4 μM.*

* Schreiber, BM. et al. Biochem J. 1999 Nov 15; 344 Pt 1:7-13

Size
80.00 USD 10µg
195.00 USD 50µg
280.00 USD 100µg
490.00 USD 250µg
840.00 USD 500µg
1,400.00 USD 1mg
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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.

Source: E.coli

Synonyms: None

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

Purity: Greater than 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.

Note:

1mg will be provided as 2x500μg.

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195.00 USD 100µg
385.00 USD 250µg
660.00 USD 500µg
1,100.00 USD 1mg
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Recombinant Human B7-1 Fc

B7-1 and B7-2 are transmembrane glycoproteins of the immunoglobulin superfamily that are expressed, along with the receptors CD28 and CTLA4, by antigen-presenting cells, and along with these receptors, constitute crucial co-stimulatory pathways for T and B cell regulatory responses. As members of the B7 family, B7-1 and B7-2 play principal roles in immunity, activating immune response and maintaining immune tolerance through engagement with CD28 and CTLA4. Co-stimulatory signals generated by B7-1 and B7-2 interactions with CD28 serve to stimulate T cell activation and prevent anergy through the amplification of T cell receptor (TCR) signaling. In contrast, interactions of the ligands with CTLA-4 serves to maintain T cell homeostasis and self-tolerance through the disruption of stimulatory signaling from B7 isoform bound CD28 complexes, and by inducing powerful inhibitory signals in T cells. B7-1 plays an important role in immune response through its amplification and regulation of T cell activity at peripheral inflammation sites. B7-1, like CTLA-4, is, however, only poorly expressed on resting dendritic cells, and its up-regulation is, therefore, considerably delayed upon immune activation. Conversely, B7-2 and CD28 are constitutively expressed by resting hematopoietic and T cells, respectively, and as a result are able to rapidly induce up-regulation upon immune activation, making them critical to the early co-stimulatory singling of immune response. Both B7-1 and B7-2 have been shown to demonstrate co-stimulatory activity in T-cell proliferation in vitro and elicit enhanced antitumor immune response in vivo. Recombinant Human B7-1Fc is a homodimeric B7-1 fusion protein, whose monomer contains a total of 441 amino acid residues, consisting of 211 amino acid residues corresponding to the extracellular domain of human B7-1, fused to the Fc portion of human IgG1. The calculated molecular weight of the B7-1 Fc monomer is 50.0 kDa.

Source: CHO cells

Synonyms: B7, BB1, CD80

AA Sequence (monomer): VIHVTKEVKE VATLSCGHNV SVEELAQTRI YWQKEKKMVL TMMSGDMNIW PEYKNRTIFD ITNNLSIVIL ALRPSDEGTY ECVVLKYEKD AFKREHLAEV TLSVKADFPT PSISDFEIPT SNIRRIICST SGGFPEPHLS WLENGEELNA INTTVSQDPE TELYAVSSKL DFNMTTNHSF MCLIKYGHLR VNQTFNWNTT KQEHFPDNGG PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG K

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

AA Sequence: Determined by its ability to inhibit alkaline phosphatase activity in differentiating MC3T3/E1 cells. The expected ED50 for this effect is 0.5-1.5 μg/ml.

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 B7-2 Fc

B7-1 and B7-2 are transmembrane glycoproteins of the immunoglobulin superfamily that are expressed, along with the receptors CD28 and CTLA4, by antigen-presenting cells, and along with these receptors, constitute crucial co-stimulatory pathways for T and B cell regulatory responses. As members of the B7 family, B7-1 and B7-2 play principal roles in immunity, activating immune response and maintaining immune tolerance through engagement with CD28 and CTLA4. Co-stimulatory signals generated by B7-1 and B7-2 interactions with CD28 serve to stimulate T cell activation and prevent anergy through the amplification of T cell receptor (TCR) signaling. In contrast, interactions of the ligands with CTLA-4 serves to maintain T cell homeostasis and self-tolerance through the disruption of stimulatory signaling from B7 isoform bound CD28 complexes, and by inducing powerful inhibitory signals in T cells. B7-1 plays an important role in immune response through its amplification and regulation of T cell activity at peripheral inflammation sites. B7-1, like CTLA-4, is, however, only poorly expressed on resting dendritic cells, and its up-regulation is, therefore, considerably delayed upon immune activation. Conversely, B7-2 and CD28 are constitutively expressed by resting hematopoietic and T cells, respectively, and as a result are able to rapidly induce up-regulation upon immune activation, making them critical to the early co-stimulatory signaling of immune response. Both B7-1 and B7-2 have been shown to demonstrate co-stimulatory activity in T-cell proliferation in vitro and elicit enhanced antitumor immune response in vivo. Recombinant Human B7-2Fc is a homodimeric B7-2 fusion protein, whose monomer contains a total of 453 amino acid residues, consisting of 222 amino acid residues corresponding to the extracellular domain of human B7-2, fused to the Fc portion of human IgG1. The calculated molecular weight of the B7-2 Fc monomer is 51.2 kDa.

Source: CHO cells

Synonyms: B70, CD86, ETC1

AA Sequence (monomer): LKIQAYFNET ADLPCQFANS QNQSLSELVV FWQDQENLVL NEVYLGKEKF DSVHSKYMGR TSFDSDSWTL RLHNLQIKDK GLYQCIIHHK KPTGMIRIHQ MNSELSVLAN FSQPEIVPIS NITENVYINL TCSSIHGYPE PKKMSVLLRT KNSTIEYDGV MQKSQDNVTE LYDVSISLSV SFPDVTSNMT IFCILETDKT RLLSSPFSIE LEDPQPPPDH 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: Greater than 95% by SDS-PAGE gel and HPLC analyses.

Biological Activity: Determined by its ability to inhibit alkaline phosphatase activity in differentiating MC3T3/E1 cells. The expected ED50 for this effect is 0.5-1.5 μg/ml.

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 B7-H2 Fc

B7-H2, or inducible costimulator-ligand (ICOSL), is a transmembrane, co-stimulatory ligand of the T cell-specific surface receptor Inducible T-cell costimulator (ICOS) that belongs to the B7 family and immunoglobulin superfamily, along with B7-1, B7-2, PD-L1 (B7-H1) and PD-L2. Whereas expression of inducible B7-1 and B7-2 is largely confined to specialized antigen-presenting cells of lymphoid tissues, B7-H2 expression occurs constitutively in hematopoietic and non-hematopoietic cells of peripheral organs. This striking difference in expression indicates that these three B7 ligands may enable temporally and spatially specific regulation of T cell response through non-competitive CD28 interaction; marking a unique function of B7-H2 in immune reactions of nonlymphoid organs in which T cells have migrated to peripheral tissues having only limited expression of B7-1 and B7-2. Expression of B7-H2 has been shown to be differentially regulated by both TNF-α and IL-1β, and inducible to a lesser extent by CD40 or lipopolysaccharide stimulation. B7-H2’s binding to ICOS on activated T cells results in both positive and negative effects on immune response, including its own downregulation. As a member of the immunoglobulin superfamily, B7-H2 is crucially involved in inflammatory immune reactions and the control of excessive immune response; however, unlike B7-1 and B7-2, B7-H2 has not been shown to influence immunity through interaction with CTLA-4, and has only been shown to have restricted interaction with CD28. Interaction of B7-H2 with ICOS has been identified as a critical event in the immunosuppression of tumor-associated memory CD4+ T cells, and has been linked to various auto-immune disorders. PeproTech’s CHO cell-derived Recombinant Human B7-H2 Fc is a glycosylated, disulfide-linked homodimer of 942 amino acid residues whose monomer consists of the 238-amino-acid length extracellular portion of B7-H2 fused to the 231-amino-acid length Fc portion of human IgG1 by two glycines. The calculated molecular weight of Recombinant Human B7-H2 Fc dimer is 104.9 kDa; however, due to glycosylation, it migrates at an apparent molecular weight of approximately 90-95 kDa by SDS-PAGE analysis under reducing conditions.

Source: CHO cells

Synonyms: Inducible Costimulator-Ligand (ICOSL), B7 homolog 2, B7-like protein Gl50, B7-related protein 1 (B7RP-1), CD275

AA Sequence (monomer): DTQEKEVRAM VGSDVELSCA CPEGSRFDLN DVYVYWQTSE SKTVVTYHIP QNSSLENVDS RYRNRALMSP AGMLRGDFSL RLFNVTPQDE QKFHCLVLSQ SLGFQEVLSV EVTLHVAANF SVPVVSAPHS PSQDELTFTC TSINGYPRPN VYWINKTDNS LLDQALQNDT VFLNMRGLYD VVSVLRIART PSVNIGCCIE NVLLQQNLTV GSQTGNDIGE RDKITENPVS TGEKNAATGG PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPG K

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

Biological Activity: Determined by its ability to induce adhesion in Jurkat cells activated by immobilized anti-CD3. The ED50 for this effect is 0.3-0.6 μg/ml.

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600.00 USD 100µg
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Recombinant Human BD-1 (36 a.a.)

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 Human BD-1 is a 3.9 kDa protein containing 36 amino acid residues.

Source: E.coli

Synonyms: Beta-Defensin 1, DEFB1, HBD1

AA Sequence: DHYNCVSSGG QCLYSACPIF TKIQGTCYRG KAKCCK

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

Biological Activity: Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100.0-1000.0 ng/ml.

Size
80.00 USD 5µg
195.00 USD 20µg
600.00 USD 100µg
1,050.00 USD 250µg
1,800.00 USD 500µg
3,000.00 USD 1mg
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Recombinant Human BD-1 (47 a.a.)

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 Human BD-1 is a 5.0 kDa protein containing 47 amino acid residues.

Source: E.coli

Synonyms: Beta-Defensin 1, DEFB1, HBD1

AA Sequence: GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK

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

Biological Activity: Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100.0-1000.0 ng/ml.

Catalog Number: 300-49
Size
80.00 USD 5µg
195.00 USD 20µg
360.00 USD 50µg
600.00 USD 100µg
1,050.00 USD 250µg
1,800.00 USD 500µg
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Recombinant Human BD-2

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 Human BD-2 is a 4.3 kDa protein containing 41 amino acid residues.

Source: E.coli

Synonyms: DEFB2, DEFB4A, Beta-Defensin 2, Skin-antimicrobial peptide 1, SAP1

AA Sequence: GIGDPVTCLK SGAICHPVFC PRRYKQIGTC GLPGTKCCKK P

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

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

Size
80.00 USD 5µg
195.00 USD 20µg
600.00 USD 100µg
1,050.00 USD 250µg
1,800.00 USD 500µg
3,000.00 USD 1mg
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Recombinant Murine BD-2

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-2 is a 5.5 kDa protein containing 51 amino acid residues.

Source: E.coli

Synonyms: Beta-Defensin 2, DEFB2, DEFB4A, Skin-Antimicrobial Peptide 1, SAP1

AA Sequence: AVGSLKSIGY EAELDHCHTN GGYCVRAICP PSARRPGSCF PEKNPCCKYM K

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

Biological Activity: Not available.

Catalog Number: 300-52
Size
80.00 USD 5µg
195.00 USD 20µg
360.00 USD 50µg
600.00 USD 100µg
1,050.00 USD 250µg
1,800.00 USD 500µg
3,000.00 USD 1mg
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Recombinant Human 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 Human BD-3 is a 5.1 kDa protein containing 45 amino acid residues.

Source: E.coli

Synonyms: Beta-Defensin 3, DEFB3, DEFB103A

AA Sequence: GIINTLQKYY CRVRGGRCAV LSCLPKEEQI GKCSTRGRKC CRRKK

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

Biological Activity: Exhibits antimicrobial activity against gram-positive bacteria S. aureus and gram-negative P. aeruginosa and E.coli.

Catalog Number: 300-65
Size
80.00 USD 5µg
195.00 USD 20µg
600.00 USD 100µg
1,050.00 USD 250µg
1,800.00 USD 500µg
3,000.00 USD 1mg
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Recombinant Human BD-4

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.   BD-4 is expressed in the testes, stomach, uterus, neutrophils, thyroid, lungs and kidneys.  In addition to its direct antimicrobial activities, BD-4 is chemoattractant towards human blood monocytes.  Recombinant Human BD-4 is a 6.0 kDa protein containing 50 amino acid residues.

Source: E.coli

Synonyms: Beta-Defensin 104, DEFB4

AA Sequence: EFELDRICGY GTARCRKKCR SQEYRIGRCP NTYACCLRKW DESLLNRTKP

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

Biological Activity: Determined by its ability to chemoattract human monocytes using a concentration range of 0.1-100.0 ng/ml.

Catalog Number: 300-68
Size
80.00 USD 5µg
195.00 USD 20µg
600.00 USD 100µg
1,050.00 USD 250µg
1,800.00 USD 500µg
3,000.00 USD 1mg
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Recombinant Human BD-5

Defensins (α and β) 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 Human BD-5 is a 5.8 kDa protein containing 51 amino acid residues.

Source: E.coli

Synonyms: BD5, DEFB5, DEFB105a, Beta-Defensin 5

AA Sequence: GLDFSQPFPS GEFAVCESCK LGRGKCRKEC LENEKPDGNC RLNFLCCRQR I

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

Biological Activity: Testing in progress.

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 Fetuin A/AHSG

Fetuin A/AHSG is a human plasma glycoprotein belonging to the Cystatin family of protease inhibitors. It is highly expressed in embryonic cells and adult hepatocytes, and is expressed to a lesser extent in monocytes/macrophages. Fetuin A/AHSG is a major serum protein component that exerts various calcium-dependent physiological activities, and can mediate growth signaling in certain tumor cells. It also can act as a natural antagonist against specific TGF-β and BMP signaling proteins, Recombinant Human Fetuin A is a heterodimeric protein containing a 282 amino acid A chain and a 27 amino acid B chain. The calculated molecular weight of Recombinant Human Fetuin A is 32.9 kDa. Due to glycosylation, recombinant Fetuin A migrates at an apparent molecular weight of 45–55 kDa by SDS-PAGE run under non-reducing conditions.

Source: HEK293 cells

Synonyms: Alpha-2-HS-glycoprotein, Alpha-2-Z-globulin, Ba-alpha-2-glycoprotien

AA Sequence: A-Chain: APHGPGLIYR QPNCDDPETE EAALVAIDYI NQNLPWGYKH TLNQIDEVKV WPQQPSGELF EIEIDTLETT CHVLDPTPVA RCSVRQLKEH AVEGDCDFQL LKLDGKFSVV YAKCDSSPDS AEDVRKVCQD CPLLAPLNDT RVVHAAKAAL AAFNAQNNGS NFQLEEISRA QLVPLPPSTY VEFTVSGTDC VAKEATEAAK CNLLAEKQYG FCKATLSEKL GGAEVAVTCT VFQTQPVTSQ PQPEGANEAV PTPVVDPDAP PSPPLGAPGL PPAGSPPDSH VL

B-Chain: TVVQPSVG AAAGPVVPPC PGRIRHFKV

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

Biological Activity: Determined by its ability to inhibit Cathespin V cleavage of a fluorogenic peptide substrate Z-LR-AMC (RLUs). The expected IC50 is ≤ 100nM.

Size
80.00 USD 200µg
195.00 USD 1mg
700.00 USD 5mg
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Recombinant Human GLP-1

GLP-1 is a proglucagon-derived peptide hormone secreted primarily by intestinal L cells during feeding. Its major physiological function is the stimulation of pancreatic β cells to release appropriate amounts of insulin after glucose absorption. Other biological actions exhibited by GLP-1 include the suppression of plasma glucagon levels, inhibition of gastric motility, and promotion of satiety. The secretion of GLP-1 from intestinal L cells is stimulated by nutrients, hormones, and neural inputs. On the other hand, insulin has been reported to inhibit GLP-1 release, indicating that a feedback loop mechanism regulates GLP-1 secretion. In addition to being the precursor of GLP-1, proglucagon, whose primary structure is highly conserved in mammalian species, is also the precursor for other members of the glucagon family of peptide hormones, including glicentin-related pancreatic peptide (GRPP), glucagons, and GLP-2. Recombinant Human GLP-1 is a 3.3 kDa polypeptide consisting of 31 amino acid residues.

Source: E.coli

Synonyms: Glucagon-Like Peptide 1

AA Sequence: HAEGTFTSDV SSYLEGQAAK EFIAWLVKGR G

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

Biological Activity: Not available.

Size
80.00 USD 2µg
195.00 USD 10µg
624.00 USD 50µg
1,040.00 USD 100µg
1,820.00 USD 250µg
3,120.00 USD 500µg
5,200.00 USD 1mg
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Recombinant Human/Murine/Rat Irisin

Irisin is a proteolytic hormone released into circulation by skeletal muscle tissue during acute exercise, and is a derivative of the cleaved plasma membrane protein Fibronectin type III domain-containing protein 5 (FNDC5). Found in muscle tissue, FNDC5 is synthesized at increased levels during exercise as a result of the overexpression of the exercise-responsive transcriptional co-activator PGC-1α (peroxisome proliferator-activated receptor-γ co-activator-1α). Like its parent polypeptide, Irisin can induce the browning of subcutaneous adipocytes, or the conversion of white adipose tissue (WAT or white fat) into brown (or beige) adipose tissue (BAT or brown fat). Given that brown fat can undergo thermogenesis, or the physiologic process of heat production, Irisin contributes to the metabolic process by increasing thermogenic function and glucose homeostasis. Irisin, thus, represents a link between exercise and “burning” of fats and/or sugars, and consequently may have relevance in the development of new treatments for diabetes and obesity. CHO cell-derived Recombinant Human/Murine/Rat Irisin is a glycosylated homodimer of 224 amino acid residues, whose monomer consists of 112 amino acid residues corresponding to the active portion of the 121-amino-acid length Irisin extracellular domain. Recombinant Human/Murine/Rat Irisin, appears to form a non-disulfide linked oligomeric structure in solution, has a calculated theoretical molecular weight of 25.2 kDa, but migrates at an apparent molecular weight of 28 kDa by SDS-PAGE analysis under reducing conditions due to glycosylation.

Source: CHO cells

Synonyms: Fibronectin type III domain-containing protein 5 (FNDC5), Fibronectin type III repeat-containing protein 2 (FRCP2)

AA Sequence (monomer): DSPSAPVNVT VRHLKANSAV VSWDVLEDEV VIGFAISQQK KDVRMLRFIQ EVNTTTRSCA LWDLEEDTEY IVHVQAISIQ GQSPASEPVL FKTPREAEKM ASKNKDEVTM KE

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

Biological Activity: Not available.

Size
80.00 USD 5µg
195.00 USD 25µg
600.00 USD 100µg
1,050.00 USD 250µg
1,800.00 USD 500µg
3,000.00 USD 1mg
Looking for a custom size?
Contact Us

Recombinant Human KLF4-TAT

KLF4 is a member of the Kruppel-like factor (KLF) family of zinc finger transcription factors. Members of this family share 3 contiguous C2H2-type zinc fingers at the carboxyl terminus that comprise the DNA-binding domain. KLF4 is highly expressed in skin and gut epithelial tissues, but is also found in various other cells and tissues, including vascular endothelial cells, lymphocytes, lung, and testis. It is an important regulator of the cell cycle, transcription, and cell differentiation. Together with Sox2, Oct4, and cMyc, KLF4 can induce the reprogramming of primary human fibroblasts to a pluripotent state. KLF4 and other transcription factors can be introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing transcription factors into primary, as well as transformed, cells. Recombinant Human KLF4-TAT is a 483 amino acid protein, including a 13-residue C-terminal TAT peptide, with a calculated molecular weight of 51.7 kDa. PeproTech’s Recombinant Human KLF4-TAT is a mixture of the expected sequence beginning at Met1 and a truncated isoform beginning at Tyr54. Due to post-translational modifications, SDS-PAGE gel shows bands at approximately 72 and 66kDa, under reduced conditions.

Source: HEK293 cells

Synonyms: Kruppel-like factor-4, EZF, GKLF

AA Sequence: MAVSDALLPS FSTFASGPAG REKTLRQAGA PNNRWREELS HMKRLPPVLP GRPYDLAAAT VATDLESGGA GAACGGSNLA PLPRRETEEF NDLLDLDFIL SNSLTHPPES VAATVSSSAS ASSSSSPSSS GPASAPSTCS FTYPIRAGND PGVAPGGTGG GLLYGRESAP PPTAPFNLAD INDVSPSGGF VAELLRPELD PVYIPPQQPQ PPGGGLMGKF VLKASLSAPG SEYGSPSVIS VSKGSPDGSH PVVVAPYNGG PPRTCPKIKQ EAVSSCTHLG AGPPLSNGHR PAAHDFPLGR QLPSRTTPTL GLEEVLSSRD CHPALPLPPG FHPHPGPNYP SFLPDQMQPQ VPPLHYQELM PPGSCMPEEP KPKRGRRSWP RKRTATHTCD YAGCGKTYTK SSHLKAHLRT HTGEKPYHCD WDGCGWKFAR SDELTRHYRK HTGHRPFQCQ KCDRAFSRSD HLALHMKRHF GGYGRKKRRQ RRR

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

Biological Activity: Testing in Progress.

Note:

100μg is the largest vial size for this product.
Larger sizes supplied as multiple 50μg and/or 100μg vials.

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