RUO Cytokines

Proteases

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.  

PeproTech’s protease products are fully purified recombinant proteins, which are free from any contaminating proteins or activities that could yield ambiguous results or otherwise complicate analyses. These products are fully tested for activity and specificity, and most are produced by an animal-free process. The products listed here contain the proteases currently available from PeproTech. This list is continually being updated, so if you don’t see the protease product that you need, please contact us.

Size

80.00 USD 100µg
195.00 USD 500µg
250.00 USD 1mg
Looking for a custom size?
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Recombinant Aeromonas Aminopeptidase

SKU: 100-10

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.  Recombinant Aeromonas Aminopeptidase is a 31.4 kDa protein containing 291 amino acid residues.

Source: E.coli

Synonyms: None

AA Sequence: MPPITQQATV TAWLPQVDAS QITGTISSLE SFTNRFYTTT SGAQASDWIA SEWQALSASL PNASVKQVSH SGYNQKSVVM TITGSEAPDE WIVIGGHLDS TIGSHTNEQS VAPGADDDASGIAAVTEVIR VLSENNFQPK RSIAFMAYAA EEVGLRGSQD LANQYKSEGK NVVSALQLDM TNYKGSAQDV VFITDYTDSN FTQYLTQLMD EYLPSLTYGF DTCGYACSDH ASWHNAGYPAAMPFESKFND YNPRIHTTQD TLANSDPTGS HAKKFTQLGL AYAIEMGSAT G

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

Biological Activity: Sequentially cleaves N-terminal amino acids except E, D, and X-P.

Note:

1mg will be provided as 2x500μg.

Size

80.00 USD 5µg
195.00 USD 25µg
360.00 USD 50µg
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 Rat Carboxypeptidase-B

SKU: 400-00

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. Carboxypeptidase-B sequentially cleaves C-terminal K and R residues. Recombinant Rat Carboxypeptidase-B is a 35.1 kDa protein consisting of 307 amino acids.

Source: E.coli

Synonyms: Cpb1

AA Sequence: ASGHSYTKYN NWETIEAWIQ QVATDNPDLV TQSVIGTTFE GRNMYVLKIG KTRPNKPAIF IDCGFHAREW ISPAFCQWFV REAVRTYNQE IHMKQLLDEL DFYVLPVVNI DGYVYTWTKD RMWRKTRSTM AGSSCLGVDP NRNFNAGWCE VGASRSPCSE TYCGPAPESE KETKALADFI RNNLSTIKAY LTIHSYSQMM LYPYSYDYKL PENYEELNAL VKGAAKELAT LHGTKYTYGP GATTIYPAAG GSDDWSYDQG IKYSFTFELR DTGFFGFLLP ESQIRQTCEE TMLAVKYIAN YVREHLY

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

Biological Activity: Carboxypeptidase-B sequentially cleaves C terminal K and R residues.

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 Enterokinase

SKU: 450-48C

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.

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

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

Size

80.00 USD 2µg
195.00 USD 10µg
576.00 USD 50µg
960.00 USD 100µg
1,680.00 USD 250µg
2,880.00 USD 500µg
4,800.00 USD 1mg
Looking for a custom size?
Contact Us

Recombinant Human Furin

SKU: 450-47

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.  Furin is a calcium-dependent serine endoprotease that processes numerous proproteins of different secretory pathways into their mature forms by cleaving at the carboxyl side of the recognition sequence, R-Xaa-(K/R)-R, where Xaa can be any amino acid.  Recombinant Human Furin is a 63.9 kDa protein, corresponding to residues 131 through 715 of the Furin precursor, plus a C-terminal His-tag.

Source: Hi-5 Insect cells

Synonyms: FUR, PACE, PCSK3

AA Sequence: DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHACSAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPEHHHHH HHH

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

Biological Activity: Measured by its ability to cleave the fluorogenic peptide substrate Boc-Arg-Val-Arg-Arg-AMC (Bachem Catalog# I-1645.0025).

Note:

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

Size

80.00 USD 50µg
195.00 USD 250µg
360.00 USD 500µg
600.00 USD 1mg
Looking for a custom size?
Contact Us

Recombinant Staphylococcus Glu-C

SKU: 450-46

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, immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, as they are frequently used in the analysis and production of proteins. Glu-C cleaves at the Carboxyl side of E (can also cleave D under certain conditions). Recombinant Staphylococcus Glu-C is a 28.8 kDa protease consisting of 266 amino acid residues.

Source: E.coli

Synonyms: V8 Protease

AA Sequence: LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLTNKHV VDATHGDPHA LKAFPSAINQ DNYPNGGFTA EQITKYSGEG DLAIVKFSPN EQNKHIGEVV KPATMSNNAE TQVNQNITVT GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP VFNEKNEVIG IHWGGVPNEF NGAVFINENV RNFLKQNIED IHFANDDQPN NPDNPDNPNN PDNPNNPDEP NNPDNPNNPD NPDNGDNNNS DNPDAA

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

Biological Activity: Cleaves at the Carboxyl side of E (can also cleave D under certain conditions).

Size

80.00 USD 2µg
195.00 USD 10µg
1,560.00 USD 100µg
2,730.00 USD 250µg
4,680.00 USD 500µg
7,800.00 USD 1mg
Looking for a custom size?
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Recombinant Murine Granzyme B

SKU: 140-03

Granzyme B is a cysteine protease found in the cytoplasmic granules of cytolytic T lymphocytes (CTL) and natural killer (NK) cells. Granzyme B is required for the induction of target cell lysis, which occurs as part of cell-mediated immune responses, and can activate apoptosis in target cells by both caspase-dependent and caspase-independent mechanisms. Proteolytic cleavage of substrates by Granzyme B takes place primarily after aspartic acid residues. Recombinant Murine Granzyme B is a glycosylated 227 amino acid protein, comprising the mature active portion of the murine Granzyme B precursor. The apparent molecular weight is 28.9 kDa by mass spectrometry.

Source: Baculovirus

Synonyms: Cytotoxic cell protease 1 (CCP1)

AA Sequence: IIGGHEVKPH SRPYMALLSI KDQQPEAICG GFLIREDFVL TAAHCEGSII NVTLGAHNIK EQEKTQQVIP MVKCIPHPDY NPKTFSNDIM LLKLKSKAKR TRAVRPLNLP RRNVNVKPGD VCYVAGWGRM APMGKYSNTL QEVELTVQKD RECESYFKNR YNKTNQICAG DPKTKRASFR GDSGGPLVCK KVAAGIVSYG YKDGSPPRAF TKVSSFLSWI KKTMKSS

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

Biological Activity: Determined by its ability to cleave a synthetic chromogentic Granzyme B substrate. The expected specific activity, when using the Ac-IEPD-pNA substrate at 25οC, is greater than 750 nM/min per μg of enzyme.

Note:

10μg is the largest vial size for this product.
Larger sizes supplied as multiple 10μg vials.

Size

80.00 USD 50µg
195.00 USD 250µg
360.00 USD 500µg
600.00 USD 1mg
Looking for a custom size?
Contact Us

Recombinant Yeast Kex-2

SKU: 450-45

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, immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, as they are frequently used in the analysis and production of proteins. Kex-2 cleaves at the carboxyl end of the recognition sequences Arg-Arg/X and Lys-Arg/X. Recombinant Yeast Kex-2 is a 60.4 kDa protease consisting of 558 amino acid residues.

Source: (BTI-Tn-5B1-4) Hi-5 Insect cells

Synonyms: Endoproteinase Lys/Arg-Arg

AA Sequence: LPVPAPPMDS SLLPVKEAED KLSINDPLFE RQWHLVNPSF PGSDINVLDL WYNNITGAGV VAAIVDDGLD YENEDLKDNF CAEGSWDFND NTNLPKPRLS DDYHGTRCAG EIAAKKGNNF CGVGVGYNAK ISGIRILSGD ITTEDEAASL IYGLDVNDIY SCSWGPADDG RHLQGPSDLV KKALVKGVTE GRDSKGAIYV FASGNGGTRG DNCNYDGYTN SIYSITIGAI DHKDLHPPYS EGCSAVMAVT YSSGSGEYIH SSDINGRCSN SHGGTSAAAP LAAGVYTLLL EANPNLTWRD VQYLSILSAV GLEKNADGDW RDSAMGKKYS HRYGFGKIDA HKLIEMSKTW ENVNAQTWFY LPTLYVSQST NSTEETLESV ITISEKSLQD ANFKRIEHVT VTVDIDTEIR GTTTVDLISP AGIISNLGVV RPRDVSSEGF KDWTFMSVAH WGENGVGDWK IKVKTTENGH RIDFHSWRLK LFGESIDSSK TETFVFGNDK EEVEPAATES TVSQYSASST SISISATSTS SISIGVETSA IPQTTTASTD PDSDPNTP

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

Biological Activity: Recombinant Kex-2 from High-5 insect cells contains the same specific activity and recognition sequence specificity as yeast derived KEX-2. 1 milligram of recombinant KEX-2 contains activity equivalent to at least 40 units of yeast derived KEX-2. Cleaves at the carboxyl side of K/R-R.

Note:

1mg will be provided as 2x500μg.

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
Looking for a custom size?
Contact Us

Recombinant Lysobacter Enzymogenes Arg-C

SKU: 450-54

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. Arg-C specifically cleaves at the carboxyl side of Arginine residues. Arg-C has a sulfhydryl requirement; it is activated by dithiothreitol, cysteine, or other sulfhydryl-containing reagents. The presence of calcium ions is essential. The enzyme is inhibited by oxidizing agents and sulfhydryl reactants, and by Co2+, Cu2+, Cd2+, and heavy metal ions. Recombinant Lysobacter Enzymogenes Arg-C is a 26.8 kDa protease consisting of 252 amino acid residues including a C-terminal His-Tag.

Source: Hi-5 Insect cells

Synonyms: None

AA Sequence: GVGDIGSSDY CEKDIVCRVK PSAEFLSASK SVARMVFTPK TGYTGYCSGT LLNNSNSPKR QLFWSAAHCI STQKVANTLQ TYWLYDATGC DNDTLSDKAV TLTGGATLLH SHATRDTLLL ELKSAPPSGA YYAGWNSSAI ATKGTAIEGI HHPSGDLKKY SLGSVTALSS TIDGKKPLTK VAWTTGVTEG GSSGSGLFTI SSTSGYQLRG GLYGGTSYCS APSDPDYYSQ LDGVWSSIKT YFSPHHHHHH HH

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

Biological Activity: The reaction is measured as an increase in absorbance at 253 nm resulting from the hydrolysis of N-benzoyl-L-arginine ethyl ester (BAEE).

Note:

20μg is the largest vial size for this product.
Larger sizes supplied as multiple 5μg and/or 20μg vials.

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
Looking for a custom size?
Contact Us

Recombinant Human MMP-1

SKU: 420-01

Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-1 is a secreted collagenase with specificity toward Type I, II, III, VII, and X collagens. Recombinant Human MMP-1 is a 42.7 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain, which is involved in substrate specificity, and in binding TIMP-1.

Source: E.coli

Synonyms: Matrix Metalloproteinase-1, Fibroblast Collagenase, Interstitial Collagenase

AA Sequence: MFVLTEGNPR WEQTHLTYRI ENYTPDLPRA DVDHAIEKAF QLWSNVTPLT FTKVSEGQAD IMISFVRGDH RDNSPFDGPG GNLAHAFQPG PGIGGDAHFD EDERWTNNFR EYNLHRVAAH ELGHSLGLSH STDIGALMYP SYTFSGDVQL AQDDIDGIQA IYGRSQNPVQ PIGPQTPKAC DSKLTFDAIT TIRGEVMFFK DRFYMRTNPF YPEVELNFIS VFWPQLPNGL EAAYEFADRD EVRFFKGNKY WAVQGQNVLH GYPKDIYSSF GFPRTVKHID AALSEENTGK TYFFVANKYW RYDEYKRSMD PGYPKMIAHD FPGIGHKVDA VFMKDGFFYF FHGTRQYKFD PKTKRILTLQ KANSWFNCRK N

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

Biological Activity: MMP-1 activity was measured by its ability to cleave a chromogenic peptide MMP-1 substrate at room temperature. At an MMP-1 concentration of 2.5 μg/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes.

Note:

1mg will be provided as 2x500μg.

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
Looking for a custom size?
Contact Us

Recombinant Human MMP-2

SKU: 420-02

Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-2 is a secreted collagenase with specificity toward Type IV, V, VII, and X collagens. Recombinant Human MMP-2 is a 62.0 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).

Source: E.coli

Synonyms: Matrix Metalloproteinase-2, Gelatinase A, TBE-1

AA Sequence: MYNFFPRKPK WDKNQITYRI IGYTPDLDPE TVDDAFARAF QVWSDVTPLR FSRIHDGEAD IMINFGRWEH GDGYPFDGKD GLLAHAFAPG TGVGGDSHFD DDELWTLGEG QVVRVKYGNA DGEYCKFPFL FNGKEYNSCT DTGRSDGFLW CSTTYNFEKD GKYGFCPHEA LFTMGGNAEG QPCKFPFRFQ GTSYDSCTTE GRTDGYRWCG TTEDYDRDKK YGFCPETAMS TVGGNSEGAP CVFPFTFLGN KYESCTSAGR SDGKMWCATT ANYDDDRKWG FCPDQGYSLF LVAAHEFGHA MGLEHSQDPG ALMAPIYTYT KNFRLSQDDI KGIQELYGAS PDIDLGTGPT PTLGPVTPEI CKQDIVFDGI AQIRGEIFFF KDRFIWRTVT PRDKPMGPLL VATFWPELPE KIDAVYEAPQ EEKAVFFAGN EYWIYSASTL ERGYPKPLTS LGLPPDVQRV DAAFNWSKNK KTYIFAGDKF WRYNEVKKKM DPGFPKLIAD AWNAIPDNLD AVVDLQGGGH SYFFKGAYYL KLENQSLKSV KFGSIKSDWL GC

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

Biological Activity: MMP-2 activity was measured by its ability to cleave a chromogenic peptide MMP-2 substrate at room temperature. At an MMP-2 concentration of 2.5 μg/ml, 50% cleavage was achieved at an incubation time of approximately 25 minutes.

Note:

1mg will be provided as 2x500μg.

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
Looking for a custom size?
Contact Us

Recombinant Human MMP-3

SKU: 420-03

Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-3 degrades fibronectin, laminin, collagens III, IV, and X, and cartilage proteoglycans. Recombinant Human MMP-3 is a 42.8 kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (378 amino acids).

Source: E.coli

Synonyms: Matrix Metalloproteinase-3, Stromelysin-1, SL-1, Transin-1

AA Sequence: MRTFPGIPKW RKTHLTYRIV NYTPDLPKDA VDSAVEKALK VWEEVTPLTF SRLYEGEADI MISFAVREHG DFYPFDGPGN VLAHAYAPGP GINGDAHFDD DEQWTKDTTG TNLFLVAAHE IGHSLGLFHS ANTEALMYPL YHSLTDLTRF RLSQDDINGI QSLYGPPPDS PETPLVPTEP VPPEPGTPAN CDPALSFDAV STLRGEILIF KDRHFWRKSL RKLEPELHLI SSFWPSLPSG VDAAYEVTSK DLVFIFKGNQ FWAIRGNEVR AGYPRGIHTL GFPPTVRKID AAISDKEKNK TYFFVEDKYW RFDEKRNSME PGFPKQIAED FPGIDSKIDA VFEEFGFFYF FTGSSQLEFD PNAKKVTHTL KSNSWLNC

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

Biological Activity: MMP-3 activity was measured by its ability to cleave a chromogenic peptide MMP-3 substrate at room temperature. At a MMP-3 concentration of 2.5 μg/ml, 50% cleavage was achieved at an incubation time of approximately 75 minutes.

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