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1000 results found for “Cofilin”
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Name :
CCNG1 HumanDescription:
Cyclin G1 Human Recombinant
Cyclin-G1, Cyclin-G, CCNG1, CCNG, CYCG1.
Product # :
PRO-1005Price :
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Description
CCNG1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-295 a.a.) and having a molecular mass of 36.2kDa. CCNG1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CCNG1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl and 5mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Cyclin-G1 (CCNG1) belongs to the cyclin family and contains the cyclin box. CCNG1 may have a part in growth regulation and is associated with G2/M phase arrest in response to DNA damage. CCNG1 may be an intermediate by which p53 mediates its role as an inhibitor of cellular proliferation. The CCNG1 protein lacks the protein destabilizing (PEST) sequence which is present in other family members.
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Synonyms
Cyclin-G1, Cyclin-G, CCNG1, CCNG, CYCG1.
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Physical Appearance
Sterile Filtered clear colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MIEVLTTTDS QKLLHQLNAL LEQESRCQPK VCGLRLIESA HDNGLRMTAR LRDFEVKDLL SLTQFFGFDT ETFSLAVNLL DRFLSKMKVQ PKHLGCVGLS CFYLAVKSIE EERNVPLATD LIRISQYRFT VSDLMRMEKI VLEKVCWKVK ATTAFQFLQL YYSLLQENLP LERRNSINFE RLEAQLKACH CRIIFSKAKP SVLALSIIAL EIQAQKCVEL TEGIECLQKH SKINGRDLTF WQELVSKCLT EYSSNKCSKP NVQKLKWIVS GRTARQLKHS YYRITHLPTI PEMVP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TINAGL1 HumanDescription:
Tubulointerstitial Nephritis Antigen Like 1 Human Recombinant
Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.
Product # :
PRO-1675Price :
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Description
800x600 TINAGL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 469 amino acids (22-467) and having a molecular mass of 52.5 kDa.TINAGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TINAGL1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Tubulointerstitial Nephritis Antigen Like 1 also known as TINAGL1 is similar in sequence to tubulointerstitial nephritis antigen, a secreted glycoprotein which is identified by antibodies in several types of immune-related tubulointerstitial nephritis. Three transcript variants encoding different isoforms are known for TINAGL1.
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Synonyms
Tubulointerstitial nephritis antigen-like isoform 1, TINAGL1, Tubulointerstitial nephritis antigen-like, Glucocorticoid-inducible protein 5, Oxidized LDL-responsive gene 2 protein, OLRG-2, Tubulointerstitial nephritis antigen-related protein, TIN Ag-related protein, TIN-Ag-RP, GIS5, LCN7, OLRG2, TINAGL, PP6614, PSEC0088, UNQ204/PRO230.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAQQGRGR RELAPGLHLR GIRDAGGRYC QEQDLCCRGR ADDCALPYLG AICYCDLFCN RTVSDCCPDF WDFCLGVPPP FPPIQGCMHG GRIYPVLGTY WDNCNRCTCQ ENRQWQCDQE PCLVDPDMIK AINQGNYGWQ AGNHSAFWGM TLDEGIRYRL GTIRPSSSVM NMHEIYTVLN PGEVLPTAFE ASEKWPNLIH EPLDQGNCAG SWAFSTAAVA SDRVSIHSLG HMTPVLSPQN LLSCDTHQQQ GCRGGRLDGA WWFLRRRGVV SDHCYPFSGR ERDEAGPAPP CMMHSRAMGR GKRQATAHCP NSYVNNNDIY QVTPVYRLGS NDKEIMKELM ENGPVQALME VHEDFFLYKG GIYSHTPVSL GRPERYRRHG THSVKITGWG EETLPDGRTL KYWTAANSWG PAWGERGHFR IVRGVNECDI ESFVLGVWGR VGMEDMGHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
KPNA2 HumanDescription:
Karyopherin Alpha 2 Human Recombinant
Karyopherin subunit alpha 2 (RAG cohort 1 importin alpha 1), RCH1, QIP2, IPOA1, SRP1 alpha, RAG cohort protein 1, importin alpha 1, importin subunit alpha-2, importin-alpha-P1, pendulin.
Product # :
PRO-1032Price :
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Description
KPNA2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 553 amino acids (1-529) and having a molecular mass of 60.5kDa.KPNA2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The KPNA2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
KPNA2 belongs to the karyopherin alpha family. KPNA2 has a vital part in the nuclear import of proteins with a conventional nuclear localization signal (NLS).
In vitro, KPNA2 bound specifically and directly to substrates having a simple or bipartite NLS motif. KPNA2 stimulated docking of import substrates to the nuclear envelope and together with Ran reconstituted complete nuclear protein import. -
Synonyms
Karyopherin subunit alpha 2 (RAG cohort 1 importin alpha 1), RCH1, QIP2, IPOA1, SRP1 alpha, RAG cohort protein 1, importin alpha 1, importin subunit alpha-2, importin-alpha-P1, pendulin.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSTNEN ANTPAARLHR FKNKGKDSTE MRRRRIEVNV ELRKAKKDDQ MLKRRNVSSF PDDATSPLQE NRNNQGTVNW SVDDIVKGIN SSNVENQLQA TQAARKLLSR EKQPPIDNII RAGLIPKFVS FLGRTDCSPI QFESAWALTN IASGTSEQTK VVVDGGAIPA FISLLASPHA HISEQAVWAL GNIAGDGSVF RDLVIKYGAV DPLLALLAVP DMSSLACGYL RNLTWTLSNL CRNKNPAPPI DAVEQILPTL VRLLHHDDPE VLADTCWAIS YLTDGPNERI GMVVKTGVVP QLVKLLGASE LPIVTPALRA IGNIVTGTDE QTQVVIDAGA LAVFPSLLTN PKTNIQKEAT WTMSNITAGR QDQIQQVVNH GLVPFLVSVL SKADFKTQKE AVWAVTNYTS GGTVEQIVYL VHCGIIEPLM NLLTAKDTKI ILVILDAISN IFQAAENLGE TEKLSIMIEE CGGLDKIEAL QNHENESVYK ASLSLIEKYF SVEEEEDQNV VPETTSEGYT FQVQDGAPGT FNF.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TPM3 HumanDescription:
Tropomyosin-3 Human Recombinant
Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.
Product # :
PRO-1020Price :
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Shipped with Ice Packs
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Description
TPM3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (1-248 a.a.) and having a molecular mass of 31.6kDa. TPM3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TPM3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, 0.1M NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Tropomyosin alpha-3 chain (TPM3) belongs to the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins which polymerize end-to-end along the major groove in most actin filaments. Tropomyosins give stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, tropomyosins regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in the TPM3 gene cause autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are linked with cancer.
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Synonyms
Tropomyosin alpha-3 chain, Gamma-tropomyosin, Tropomyosin-3, Tropomyosin-5, hTM5, TPM3, TM3, TM5, TRK, CFTD, NEM1, TM-5, TM30, TM30nm, TPMsk3, hscp30, OK/SW-cl.5.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMAGITT IEAVKRKIQV LQQQADDAEE RAERLQREVE GERRAREQAE AEVASLNRRI QLVEEELDRA QERLATALQK LEEAEKAADE SERGMKVIEN RALKDEEKME LQEIQLKEAK HIAEEADRKY EEVARKLVII EGDLERTEER AELAESRCRE MDEQIRLMDQ NLKCLSAAEE KYSQKEDKYE EEIKILTDKL KEAETRAEFA ERSVAKLEKT IDDLEDKLKC TKEEHLCTQR MLDQTLLDLN EM.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CDC37 Human, HisDescription:
Cell Division Cycle 37 Human Recombinant, His Tag
Cell Division Cycle 37 homolog, P50CDC37, CDC37, Hsp90 chaperone protein kinase-targeting subunit, CDC37 cell division cycle 37 homolog, hsp90 co-chaperone Cdc37, CDC37A.
Product # :
PRO-140Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CDC37, His Protein is a 45.71 kDa protein containing 388 amino acids fused to a 10 aa N-Terminal His-tag.
Source
E. coli
Formulation
CDC37, His Human was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in
20mM TRIS, 50mM NaCl, pH 7.5.More Info
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Introduction
CDC37, His protein is extremely parallel to Cdc 37, a cell division cycle control protein of Sacchromyces cerevisiae. CDC37 is a molecular chaperone with a detailed role in cell signal transduction. CDC37 forms a complex with Hsp90 and several protein kinases including CDK4, CDK6, SRC, RAF-1, MOK, and eIF2 alpha kinases CDC37 has a vital part in directing Hsp90 to its target kinases.
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Synonyms
Cell Division Cycle 37 homolog, P50CDC37, CDC37, Hsp90 chaperone protein kinase-targeting subunit, CDC37 cell division cycle 37 homolog, hsp90 co-chaperone Cdc37, CDC37A.
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Stability
Store lyophilized CDC37 His human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted CDC37 can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
Add deionized water to prepare a working stock solution of 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG DPLLEAVPKT GDEKDVSV
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CHI3L2 HumanDescription:
Chitinase 3-Like 2 Recombinant
Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, CHI3L2.
Product # :
ENZ-811Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
CHI3L2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Tyr27-Leu390) containing 374 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 42.1kDa.
Source
Escherichia Coli.
Formulation
CHI3L2 was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 30mM acetate buffer, pH 4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Chitinase 3-Like 2 (CHI3L2) is similar to bacterial chitinases but lacks chitinase activity. CHI3L2 protein is secreted and is involved in cartilage biogenesis. CHI3L2 is a lectin, which binds chitooligosaccharides and other glycans with high affinity.
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Synonyms
Chitinase 3-Like 2, Chondrocyte Protein 39, YKL-39, YKL39, Chitinase-3-Like Protein 2, CHIL2, CHI3L2.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add 0.1M acetate buffer pH 4.0 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited.CHI3L2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASYKLVCYFTNW SQDRQEPGKF TPENIDPFLC SHLIYSFASI ENNKVIIKDK SEVMLYQTIN SLKTKNPKLK ILLSIGGYLF GSKGFHPMVD SSTSRLEFIN SIILFLRNHN FDGLDVSWIY PDQKENTHFT VLIHELAEAF QKDFTKSTKE RLLLTAGVSA GRQMIDNSYQ VEKLAKDLDF INLLSFDFHG SWEKPLITGH NSPLSKGWQD RGPSSYYNVE YAVGYWIHKG MPSEKVVMGI PTYGHSFTLA SAETTVGAPA SGPGAAGPIT ESSGFLAYYE ICQFLKGAKI TRLQDQQVPY AVKGNQWVGY DDVKSMETKV QFLKNLNLGG AMIWSIDMDD FTGKSCNQGP YPLVQAVKRS LGSL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CNTFR RatDescription:
Ciliary Neurotrophic Factor Receptor Rat Recombinant
Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.
Product # :
CYT-959Price :
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Description
CNTFR Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 328 amino acids (23-342a.a) and having a molecular mass of 36.9kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). CNTFR is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CNTFR protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Ciliary Neurotrophic Factor Receptor, also known as CNTFR is a member of the type I cytokine receptor family. CNTFR binds to CNTF.The alpha subunit provides the receptor specificity.Sole nucleotide polymorphisms in CNTFR has been associated with variations in muscle strength, in addition to early onset of eating disorders.
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Synonyms
Ciliary neurotrophic factor receptor subunit alpha, CNTF receptor subunit alpha, CNTFR-alpha.
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Physical Appearance
Sterile Filtered colorless clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
QKHSPQEAPH VQYERLGTDV TLPCGTASWD AAVTWRVNGT DLAPDLLNGS QLILRSLELG HSGLYACFHR DSWHLRHQVL LHVGLPPREP VLSCRSNTYP KGFYCSWHLS APTYIPNTFN VTVLHGSKMM VCEKDPALKN RCHIRYMHLF STIKYKVSIS VSNALGHNTT AITFDEFTIV KPDPPENVVA RPVPSNPRRL EVTWQTPSTW PDPESFPLKF FLRYRPLILD QWQHVELSNG TAHTITDAYA GKEYIIQVAA KDNEIGTWSD WSVAAHATPW TEEPRHLTTE AQAPETTTST TSSLAPPPTT KICDPGELSS LEHHHHHH.
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Background
What is the molecular weight/Mw of CNTFR Protein?
CNTFR Protein has a total Mw of 36.9kDa.
What is the source or expression system of CNTFR Protein?
Sf9, Baculovirus cells.
What is the Purity of CNTFR Protein?
CNTFR Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTFR Protein?
The biological functionality of CNTFR Protein will be determined in the future.
What is the amino acid sequence of CNTFR Protein?
QKHSPQEAPH VQYERLGTDV TLPCGTASWD AAVTWRVNGT DLAPDLLNGS QLILRSLELG HSGLYACFHR DSWHLRHQVL LHVGLPPREP VLSCRSNTYP KGFYCSWHLS APTYIPNTFN VTVLHGSKMM VCEKDPALKN RCHIRYMHLF STIKYKVSIS VSNALGHNTT AITFDEFTIV KPDPPENVVA RPVPSNPRRL EVTWQTPSTW PDPESFPLKF FLRYRPLILD QWQHVELSNG TAHTITDAYA GKEYIIQVAA KDNEIGTWSD WSVAAHATPW TEEPRHLTTE AQAPETTTST TSSLAPPPTT KICDPGELSS LEHHHHHH.
What applications can CNTFR Protein be used in?
CNTFR Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTFR Protein?
The endotoxin level is minimal, CNTFR Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
COMMD1 HumanDescription:
Copper Metabolism Domain Containing 1 Human Recombinant
MURR1, C2orf5, COMMD1, Copper Metabolism Domain Containing 1, MGC27155.
Product # :
PRO-862Price :
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Description
COMMD1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-190 a.a.) and having a molecular mass of 23.3 kDa. The COMMD1 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
COMMD1 Human solution containing 20mM Tris pH-8, 0.1M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
COMMD1 is accountable for inhibition of TNF-induced NFκB p50 and n facilitats of biliary copper excretion within hepatocytes. High expression of COMMD1 is localized in liver tissue, with lower expressions in lung, heart, kidney and brain tissue. COMMD1 interacts directly with COMMD6 and ATP7B, and indirectly with IκB-β and COMMD7.
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Synonyms
MURR1, C2orf5, COMMD1, Copper Metabolism Domain Containing 1, MGC27155.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAGELEGGK PLSGLLNALA QDTFHGYPGI TEELLRSQLY PEVPPEEFRP FLAKMRGILK SIASADMDFN QLEAFLTAQT KKQGGITSDQ AAVISKFWKS HKTKIRESLM NQSRWNSGLR GLSWRVDGKS QSRHSAQIHT PVAIIELELG KYGQESEFLC LEFDEVKVNQ ILKTLSEVEE SISTLISQPN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
VNN1 HumanDescription:
Vanin 1 Human Recombinant
Vanin 1, Vascular Non-Inflammatory Molecule 1, Pantetheine Hydrolase, EC 3.5.1.92, Vanin-1, HDLCQ8, Tiff66, Pantetheinase, Vannin 1, EC 3.5.1, VNN1.
Product # :
PRO-2047Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
VNN1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Gln22-Gly491) containing 480 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 53.5kDa.
Source
Escherichia Coli.
Formulation
VNN1 was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl and 0.1% amisoft CS-22, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Vanin 1 (VNN1) belongs to the vanin family of proteins, which share extensive sequence similarity with each other, and also with biotinidase. This family includes secreted and membrane-associated proteins, a few of which have been described to participate in hematopoietic cell trafficking. No biotinidase activity has been established for any of the vanin proteins; nevertheless, they possess pantetheinase activity, which may have a role in oxidative-stress response. VNN1 protein, like its mouse homolog, is probably a GPI-anchored cell surface molecule. The mouse VNN1 protein is expressed by the perivascular thymic stromal cells and regulates migration of T-cell progenitors to the thymus. VNN1 is an amidohydrolase which hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5).
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Synonyms
Vanin 1, Vascular Non-Inflammatory Molecule 1, Pantetheine Hydrolase, EC 3.5.1.92, Vanin-1, HDLCQ8, Tiff66, Pantetheinase, Vannin 1, EC 3.5.1, VNN1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. VNN1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHASQDTFTAAVYE HAAILPNATL TPVSREEALA LMNRNLDILE GAITSAADQG AHIIVTPEDA IYGWNFNRDS LYPYLEDIPD PEVNWIPCNN RNRFGQTPVQ ERLSCLAKNN SIYVVANIGD KKPCDTSDPQ CPPDGRYQYN TDVVFDSQGK LVARYHKQNL FMGENQFNVP KEPEIVTFNT TFGSFGIFTC FDILFHDPAV TLVKDFHVDT IVFPTAWMNV LPHLSAVEFH SAWAMGMRVN FLASNIHYPS KKMTGSGIYA PNSSRAFHYD MKTEEGKLLL SQLDSHPSHS AVVNWTSYAS SIEALSSGNK EFKGTVFFDE FTFVKLTGVA GNYTVCQKDL CCHLSYKMSE NIPNEVYALG AFDGLHTVEG RYYLQICTLL KCKTTNLNTC GDSAETASTR FEMFSLSGTF GTQYVFPEVL LSENQLAPGE FQVSTDGRLF SLKPTSGPVL TVTLFGRLYE KDWASNASSG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
VTN HumanDescription:
Vitronectin Human Recombinant
Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.
Product # :
PRO-2008Price :
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Shipped with Ice Packs
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Description
VTN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 482 amino acids (20-478 a.a) and having a molecular mass of 54.7kDa. VTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VTN protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Vitronectin (VTN) which is a part of the pexin family is a cell adhesion and spreading factor found in serum and tissues. VTN interacts with glycosaminoglycans and proteoglycans. VTN inhibits the membrane-damaging effect of the terminal cytolytic complement pathway and binds to numerous serpin serine protease inhibitors. Scientists have been noticed an over expression of VTN, integrins and plasminogen in migrating cells during wound healing.
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Synonyms
Vitronectin precursor, V75, VN, VNT, Vitronectin, VTN, S-protein, Serum-spreading factor, Vitronectin V65 subunit, Vitronectin V10 subunit, Somatomedin-B.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDQESCKG RCTEGFNVDK KCQCDELCSY YQSCCTDYTA ECKPQVTRGD VFTMPEDEYT VYDDGEEKNN ATVHEQVGGP SLTSDLQAQS KGNPEQTPVL KPEEEAPAPE VGASKPEGID SRPETLHPGR PQPPAEEELC SGKPFDAFTD LKNGSLFAFR GQYCYELDEK AVRPGYPKLI RDVWGIEGPI DAAFTRINCQ GKTYLFKGSQ YWRFEDGVLD PDYPRNISDG FDGIPDNVDA ALALPAHSYS GRERVYFFKG KQYWEYQFQH QPSQEECEGS SLSAVFEHFA MMQRDSWEDI FELLFWGRTS AGTRQPQFIS RDWHGVPGQV DAAMAGRIYI SGMAPRPSLA KKQRFRHRNR KGYRSQRGHS RGRNQNSRRP SRATWLSLFS SEESNLGANN YDDYRMDWLV PATCEPIQSV FFFSGDKYYR VNLRTRRVDT VDPPYPRSIA QYWLGCPAPG HL.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GDF3 HumanDescription:
Growth Differentiation Factor-3 Human Recombinant
Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.
Product # :
CYT-694Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
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Description
GDF3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 124 amino acids and having a total molecular mass of 14.15 kDa.GDF3 is fused to a 10 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated solution (0.5mg/ml) containing 30mM Acetate buffer pH-4.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
GDF3 is a member of the TGF-beta superfamily though it does not show similarity pattern of conserved cysteine residues. GDF3 is linked to Vg-1 and human BMP-4. GDF3 transcripts are identified mainly in adult bone marrow, spleen, thymus, and adipose tissue. GDF3 expression is upregulated strongly in high-fat-fed C57Bl/6J FABP4/aP2 null mice, which develop obesity but not the related hyperglycemia or hyperinsulinemia characteristic of type II diabetes. GDF3 expression therefore bonds fatty acid metabolism in adipocytes and the expression of a differentiation regulator belonging to the bone morphogenetic proteins.
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Synonyms
Growth Differentiation Factor 3, Growth/Differentiation Factor 3 , MCOPCB6, MCOP7, GDF-3, KFS3.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GDF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized GDF3 in sterile 100mM Acetate buffer pH-4 at a concentration of 0.5mg/ml. For the dilution into higher pH values, it is recommended to dilute the protein to a concentration of 10μg/ml. Please note that in higher concentrations the solubility of GDF3 is limited. The protein is not sterile! Please sterile filter before using it in the cell culture.
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Amino Acid Sequence
MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.
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Background
What is the molecular weight/Mw of GDF3 HUMAN Protein?
GDF3 HUMAN Protein has a total Mw of 14.15XkDa.
What is the source or expression system of GDF3 HUMAN Protein?
Escherichia Coli.
What is the Purity of GDF3 HUMAN Protein?
GDF3 HUMAN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF3 HUMAN Protein?
The biological functionality of GDF3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GDF3 HUMAN Protein?
MKHHHHHHAS AAIPVPKLSC KNLCHRHQLF INFRDLGWHK WIIAPKGFMA NYCHGECPFS LTISLNSSNY AFMQALMHAV DPEIPQAVCI PTKLSPISML YQDNNDNVIL RHYEDMVVDECGCG.
What applications can GDF3 HUMAN Protein be used in?
GDF3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF3 HUMAN Protein?
The endotoxin level is minimal, GDF3 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
VAPA HumanDescription:
VAMP Associated Protein A 33kDa Human Recombinant
hVAP-33, VAP-33, VAP-A, VAP33, Vesicle-associated membrane protein-associated protein A, VAMP-associated protein A, VAMP-A, 33 kDa VAMP-associated protein, VAPA.
Product # :
PRO-779Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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Description
VAPA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 264 amino acids (1-227 a.a.) and having a molecular mass of 29.8 kDa. VAPA is fused to 37 amino acid His Tag and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
VAPA solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
VAPA is involved in vesicle traficking. VAPA is a type IV membrane protein. It is localized in the plasma membrane and intracellular vesicles. VAPA is related with the cytoskeleton. VAPA functions membrane fusion, protein complex assembly and cell motility. VAPA is an essential regulator both of the subcellular localization of protrudin and of its ability to stimulate neurite outgrowth.
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Synonyms
hVAP-33, VAP-33, VAP-A, VAP33, Vesicle-associated membrane protein-associated protein A, VAMP-associated protein A, VAMP-A, 33 kDa VAMP-associated protein, VAPA.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
RGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAS ASGAMAKHEQ ILVLDPPTDL KFKGPFTDVV TTNLKLRNPS DRKVCFKVKT TAPRRYCVRP NSGIIDPGST VTVSVMLQPF DYDPNEKSKH KFMVQTIFAP PNTSDMEAVW KEAKPDELMD SKLRCVFEMP NENDKLNDME PSKAVPLNAS KQDGPMPKPH SVSLNDTETR KLMEECKRLQ GEMMKLSEEN RHLRDEGLRL RKVAHSDKPG STSTASFRDN VTSP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Hepsin HumanDescription:
Hepsin Human Recombinant
HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.
Product # :
PRO-2846Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Hepsin Human Recombinant produced in Cho cells is a covalently-linked heterodimer having a total molecular mass of 43.0kDa. Hepsin is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
CHO cells.
Formulation
The Hepsin protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris and 150mM NaCl, pH 8.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity is >20,000 pmol/min/μg and was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC).More Info
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Synonyms
HPN, TMPRSS1, Serine protease hepsin, Transmembrane protease serine 1.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Hepsin Active although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hepsin Active should be stored at 4°C between 2-7 days and for future use below -18°C.
Please prevent freeze-thaw cycles. -
Solubility
It is recommended to reconstitute the lyophilized Hepsin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
Light Chain (Non-catalytic Chain)
RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR.
Heavy Chain (Catalytic Chain)
IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H.
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Background
Hepsin is a type II transmembrane serine protease expressed primarily on epithelial cells, it takes part in extracellular proteolysis by activating precursor proteins such as pro-HGF and contributes to tissue remodeling, cell signaling, and normal epithelial function. Recombinant Hepsin is used to study prostate cancer, extracellular matrix remodelling, protease signalling pathways, tumor invasion, metastasis, HGF/MET signaling, and for screening inhibitors that target serine proteases
What is the molecular weight / Mw of Hepsin Protein?
Hepsin Protein has a total Mw of 43kDa.
What is the source or expression system of Hepsin Protein?
CHO Cells
What is the Purity of Hepsin Protein?
Hepsin Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of Hepsin Protein?
The enzymatic activity was measured by its ability to cleave tert-butoxycarbonyl-Gln-Arg-Arg-7-amino-4-methylcoumarin (Boc-QRR-AMC). The specific activity is >20,000 pmol/min/μg.
What is the amino acid sequence of Hepsin Protein?
Light Chain (Non-catalytic Chain)
RSDQEPLYPV QVSSADARLM VFDKTEGTWR LLCSSRSNAR VAGLSCEEMG FLRALTHSEL DVRTAGANGT SGFFCVDEGR LPHTQRLLE VISVCDCPRGR FLAAICQDCG RRKLPVDR
Heavy Chain (Catalytic Chain)
IVGGRDTSLG RWPWQVSLRY DGAHLCGGSL LSGDWVLTAA HCFPERNRVL SRWRVFAGAV AQASPHGLQL GVQAVVYHGG YLPFRDPNSE ENSNDIALVH LSSPLPLTEY IQPVCLPAAG QALVDGKICT VTGWGNTQYY GQQAGVLQEA RVPIISNDVC NGADFYGNQI KPKMFCAGYP EGGIDACQGD SGGPFVCEDS ISRTPRWRLC GIVSWGTGCA LAQKPGVYTK VSDFREWIFQ AIKTHSEASG MVTQLHHHHH H
What applications can Hepsin Protein be used in?
Hepsin Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for Hepsin Protein?
The endotoxin level is minimal, Hepsin Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GMFB RatDescription:
Glia Maturation Factor Beta Rat Recombinant
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.
Product # :
CYT-049Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- formulation
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Description
Glia Maturation Factor-Beta (GMF-Beta) Rat Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.6kDa. GMF-Beta is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 1×PBS, pH 7.4.
Purity
Greater than 97.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.
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Synonyms
Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GMFB although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution GMFB should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized GMFB in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDKR LVVLDEELEG VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPLGCKPEQQ MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.
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Background
What is the molecular weight/Mw of GMFB RAT Protein?
GMFB RAT Protein has a total Mw of 16.6kDa.
What is the source or expression system of GMFB RAT Protein?
Escherichia Coli.
What is the Purity of GMFB RAT Protein?
GMFB RAT Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of GMFB RAT Protein?
The biological functionality of GMFB RAT Protein will be determined in the future.
What is the amino acid sequence of GMFB RAT Protein?
SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDKR LVVLDEELEG VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPLGCKPEQQ MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.
What applications can GMFB RAT Protein be used in?
GMFB RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GMFB RAT Protein?
The endotoxin level is minimal, GMFB RAT Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MIF RatDescription:
Macrophage Migration Inhibitory Factor Rat Recombinant
Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
Product # :
CYT-193Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
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Description
MIF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa. The MIF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIF should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized MIF in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTSDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
HFE HumanDescription:
Hemochromatosis Human Recombinant
Hereditary hemochromatosis protein, HLA-H, HFE, HLAH, HH, HFE1, MVCD7, TFQTL2.
Product # :
PRO-1332Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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Description
HFE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (23-306 a.a) and having a molecular mass of 35.7kDa.HFE is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HFE protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Hemochromatosis (HFE) is a member of the MHC class I family. The Hemochromatosis protein contains 1 Ig-like C1-type (immunoglobulin-like) domain. HFE is a membrane protein, which is similar to MHC class I-type proteins and associates with beta-2 microglobulin (beta2M). It is assumed that the HFE protein acts to regulate iron absorption by regulating the interaction of the transferrin receptor (TFR) with transferrin. HFE binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin.
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Synonyms
Hereditary hemochromatosis protein, HLA-H, HFE, HLAH, HH, HFE1, MVCD7, TFQTL2.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMRLLRSH SLHYLFMGAS EQDLGLSLFE ALGYVDDQLF VFYDHESRRV EPRTPWVSSR ISSQMWLQLS QSLKGWDHMF TVDFWTIMEN HNHSKESHTL QVILGCEMQE DNSTEGYWKY GYDGQDHLEF CPDTLDWRAA EPRAWPTKLE WERHKIRARQ NRAYLERDCP AQLQQLLELG RGVLDQQVPP LVKVTHHVTS SVTTLRCRAL NYYPQNITMK WLKDKQPMDA KEFEPKDVLP NGDGTYQGWI TLAVPPGEEQ RYTCQVEHPG LDQPLIVIWE PSPSGTLV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
AIFM1 HumanDescription:
Apoptosis-Inducing Factor, Mitochondrion-Associated, 1 Human Recombinant
Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 1.
Product # :
PRO-1898Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Description
AIFM1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 537 amino acids (98-609) and having a molecular mass of 58.5 kDa.AIFM1 is fused to a 25 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AIFM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Apoptosis-Inducing Factor, Mitochondrion-Associated, 1 (AIFM1) is a mitochondrial protein which translocates to the nucleus once apoptosis has been initiated. AIFM1 causes DNA fragmentation and chromatin condensation and also triggers the release of cytochrome c and caspase-9 from mitochondria. Bcl-2 overexpression prevents the release of AIFM1 from mitochondria, but doesn’t block its apoptogenic activity.
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Synonyms
Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFLGLTP EQKQKKAALS ASEGEEVPQD KAPSHVPFLL IGGGTAAFAA ARSIRARDPG ARVLIVSEDP ELPYMRPPLS KELWFSDDPN VTKTLRFKQW NGKERSIYFQ PPSFYVSAQD LPHIENGGVA VLTGKKVVQL DVRDNMVKLN DGSQITYEKC LIATGGTPRS LSAIDRAGAE VKSRTTLFRK IGDFRSLEKI SREVKSITII GGGFLGSELA CALGRKARAL GTEVIQLFPE KGNMGKILPE YLSNWTMEKV RREGVKVMPN AIVQSVGVSS GKLLIKLKDG RKVETDHIVA AVGLEPNVEL AKTGGLEIDS DFGGFRVNAE LQARSNIWVA GDAACFYDIK LGRRRVEHHD HAVVSGRLAG ENMTGAAKPY WHQSMFWSDL GPDVGYEAIG LVDSSLPTVG VFAKATAQDN PKSATEQSGT GIRSESETES EASEITIPPS TPAVPQAPVQ GEDYGKGVIF YLRDKVVVGI VLWNIFNRMP IARKIIKDGE QHEDLNEVAK LFNIHED.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IGF1 Gilthead SeabreamDescription:
IGF1 Gilthead Seabream Recombinant
Somatomedin C, IGF-I, IGFI.
Product # :
CYT-295Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IGF1 Gilthead SeabreamRecombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7545.4 Dalton, the predicted pI=7.72.IGF-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.More Info
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Introduction
The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2), and somatomedin B.
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Synonyms
Somatomedin C, IGF-I, IGFI.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized IGF-1 in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK
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Background
What is the molecular weight/Mw of IGF1 GILTHEAD SEABREAM Protein?
IGF1 GILTHEAD SEABREAM Protein has a total Mw of 7.54kDa.
What is the source or expression system of IGF1 GILTHEAD SEABREAM Protein?
Escherichia Coli.
What is the Purity of IGF1 GILTHEAD SEABREAM Protein?
IGF1 GILTHEAD SEABREAM Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IGF1 GILTHEAD SEABREAM Protein?
Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.
What is the amino acid sequence of IGF1 GILTHEAD SEABREAM Protein?
MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK
What applications can IGF1 GILTHEAD SEABREAM Protein be used in?
IGF1 GILTHEAD SEABREAM Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGF1 GILTHEAD SEABREAM Protein?
The endotoxin level is minimal, IGF1 GILTHEAD SEABREAM Protein was purified using conventional chromatography techniques.
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Protein content
Somatomedin C quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.60 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IGF1 as a Reference Standard.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NRG1 A HumanDescription:
Neuregulin-1/Heregulin Alpha (EGF Domain) Human Recombinant
Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.
Product # :
CYT-736Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Neuregulin-1/Heregulin Alpha (EGF Domain) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 65 amino acids and having a total molecular mass of 7.4kDa. NRG1-A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered solution in 20mM PB, pH 6.0 and 150mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is less than 40 ng/ml, corresponding to a specific activity of > 2.5×104 units/mg.More Info
-
Introduction
Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. These isoforms contain the heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). All these factors have the Ig and EGF-like domain, and are able to bind to ErbB3 and ErbB4 receptor tyrosin kinases. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. NRG1 isoforms act to induce the growth and differentiation of epithelial, neuronal, glial, and other types of cells.
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Synonyms
Neuregulin-1, Heregulin Alpha, NRG1-A, NRG1 A.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized NRG1-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRG1-A should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized NRG1-A in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCQPGF TGARCTENVP MKVQNQEKAE ELYQK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PLGF2 Human, CHODescription:
Placental Growth Factor-2 Human Recombinant, CHO
PIGF, PGF, PlGF-2, PLGF-2.
Product # :
CYT-868Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PLGF2 Human Recombinant (19-170 a.a.) produced in CHO is a disulfide-linked homodimeric, glycosylated, polypeptide chain containing 152 amino acids and having a molecular mass of 33kDa.The PLGF-2 Human Recombinant protein is purified by proprietary chromatographic techniques.
Source
Chinese Hamster Ovary cells (CHO).
Formulation
PLGF-2 protein was lyophilized from a 0.2µm filtered solution in HCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, as measured in a cell proliferation assay using MDA?MB?231 cells is less than 10µg/ml.More Info
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Introduction
PLGF is a growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration. It binds to receptor vegfr-1/flt1.
PLGF-2 binds neuropilin-1 and 2 in a heparin-dependent manner. -
Synonyms
PIGF, PGF, PlGF-2, PLGF-2.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized PLGF-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PLGF2 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized PLGF2 at 200µg/ml in PBS, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
LPAVPPQQWA LSAGNGSSEV EVVPFQEVWG RSYCRALERL VDVVSEYPSE VEHMFSPSCV SLLRCTGCCG DENLHCVPVE TANVTMQLLK IRSGDRPSYV ELTFSQHVRC ECRPLREKMK PERRRPKGRG KRRREKQRPT DCHLCGDAVP RR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LAIR2 HumanDescription:
Leukocyte-Associated Ig-Like Receptor 2 Human Recombinant
Leukocyte-associated immunoglobulin-like receptor 2, LAIR-2, CD306, LAIR2.
Product # :
PRO-1081Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LAIR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (22-135 a.a) and having a molecular mass of 15.2kDa.LAIR2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LAIR2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Leukocyte-associated immunoglobulin-like receptor 2 (LAIR2) is a secreted, 131 amino acids protein which contains one IglikeC2 type domain, rendering it a member of the Ig superfamily. Even though one is secreted and one is membrane bound, the 2 LAIR proteins are assumed to have evolved from a common gene ancestor and seem to share similar adhesion profiles, suggesting that LAIR2 may compete with LAIR1 for ligand binding. LAIR2 was discovered by its similarity to LAIR1, which is an inhibitory receptor present on mononuclear leukocytes. The LAIR2 gene maps to a region of 19q13.4, dubbed the leukocyte receptor cluster, which contains 29 genes in the immunoglobulin superfamily, including LAIR1. The function of the LAIR2 protein is unknown, though it is assumed to be secreted and may help modulate mucosal tolerance.
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Synonyms
Leukocyte-associated immunoglobulin-like receptor 2, LAIR-2, CD306, LAIR2.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMQEGAL PRPSISAEPG TVISPGSHVT FMCRGPVGVQ TFRLEREDRA KYKDSYNVFR LGPSESEARF HIDSVSEGNA GLYRCLYYKP PGWSEHSDFL ELLVKGTVPG TEASGFDAP.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
M CSF HumanDescription:
Macrophage-Colony Stimulating Factor Human Recombinant
Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
Product # :
CYT-308Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a disulfide linked homodimer, non-glycosylated, polypeptide chain containing 2 x 159 amino acids and having a total molecular mass of 37.1 KD. MCSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MCSF protein was lyophilized with 10mM sodium Phosphate, pH-8.0 & 50mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50, calculated by the dose-dependent stimulation of the proliferation of murine M-NFS-60 indicator cells was found to be 1.15ng/ml corresponding to a specific activity of 8.7x105 Units/mg.
More Info
-
Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. MCSF induces cells of the monocyte/macrophage lineage. MCSF plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
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Synonyms
Macrophage Colony Stimulating Factor, CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MCSF should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized MCSF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ GHERQSEGS.
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Background
M-CSF (Macrophage-Colony Stimulating Factor) Human Recombinant: Unraveling Its Role in Macrophage Biology and Beyond
Abstract:
M-CSF (Macrophage-Colony Stimulating Factor), also known as Lanimostim, MCSF, or MGC31930, is a crucial growth factor that regulates the development, proliferation, and function of macrophages.
This research paper aims to provide a comprehensive analysis of the molecular characteristics, signaling pathways, and diverse physiological functions of M-CSF. Additionally, it explores the therapeutic implications of M-CSF in various diseases and disorders.
Synonyms such as Lanimostim, MCSF, and MGC31930 associated with the protein are discussed throughout the paper to highlight their relevance in scientific literature.
Introduction:
- M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a growth factor that plays a critical role in the regulation of macrophage biology. This section introduces M-CSF and its synonyms, highlighting their significance and relevance in scientific research.
Molecular Characteristics of M-CSF:
- This section explores the molecular characteristics of M-CSF, including its primary amino acid sequence, protein structure, and post-translational modifications. The importance of these factors in determining M-CSF's biological activity and receptor binding is discussed.
Signaling Pathways Activated by M-CSF:
- M-CSF activates specific signaling pathways upon binding to its receptor, leading to diverse cellular responses. This section focuses on the activation of the MAPK/ERK and PI3K/Akt pathways. The downstream effectors and transcriptional regulators involved in mediating M-CSF's cellular responses are also discussed.
Physiological Functions of M-CSF:
- M-CSF plays critical roles in various physiological processes, particularly in macrophage development, survival, polarization, and immune regulation. This section provides an in-depth analysis of M-CSF's contributions to these processes, emphasizing its role in hematopoiesis, tissue homeostasis, wound healing, and host defense.
Therapeutic Implications of M-CSF:
- The unique properties of M-CSF make it a promising therapeutic candidate for various diseases and disorders. This section discusses the potential applications of M-CSF in immunotherapy, tissue regeneration, cancer treatment, and autoimmune diseases. The challenges and future directions in utilizing M-CSF as a therapeutic agent are also explored.
M-CSF in Disease Pathogenesis:
- M-CSF dysregulation is implicated in the pathogenesis of several diseases, including cancer, inflammation, and bone disorders. This section examines the role of M-CSF in promoting tumor progression, macrophage-mediated inflammation, osteoclast differentiation, and metabolic diseases. The therapeutic implications and targeting of M-CSF in disease management are also discussed.
Conclusion:
- M-CSF, also known as Lanimostim, MCSF, or MGC31930, is a critical growth factor involved in macrophage biology and disease pathogenesis. Understanding the molecular characteristics, signaling pathways, and physiological functions of M-CSF contributes to the exploration of its therapeutic potential in various disorders.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CCL14 Human (66 a.a.)Description:
HCC-1 Human Recombinant (CCL14) (66 a.a.)
Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.
Product # :
CHM-006Price :
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Shipped at Room temp
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Description
HCC-1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 66 amino acids and having a molecular mass of 7.8kDa. The HCC-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CCL14 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4 and 5% trehalose.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological activity is determined by its ability to chemoattract human monocytes using a concentration range of 5.0-20.0 ng/ml.More Info
-
Introduction
Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.
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Synonyms
Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized HCC1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL14 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized HCC-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
GPYHPSECCF TYTTYKIPRQ RIMDYYETNS QCSKPGIVFI TKRGHSVCTN PSDKWVQDYI KDMKEN.
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Background
What is the molecular weight/Mw of CCL14 HUMAN (66 A.A.) Protein?
CCL14 HUMAN (66 A.A.) Protein has a total Mw of 7.8kDa.
What is the source or expression system of CCL14 HUMAN (66 A.A.) Protein?
Escherichia Coli.
What is the Purity of CCL14 HUMAN (66 A.A.) Protein?
CCL14 HUMAN (66 A.A.) Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL14 HUMAN (66 A.A.) Protein?
The Biological activity is determined by its ability to chemoattract human monocytes using a concentration range of 5.0-20.0 ng/ml.
What is the amino acid sequence of CCL14 HUMAN (66 A.A.) Protein?
GPYHPSECCF TYTTYKIPRQ RIMDYYETNS QCSKPGIVFI TKRGHSVCTN PSDKWVQDYI KDMKEN.
What applications can CCL14 HUMAN (66 A.A.) Protein be used in?
CCL14 HUMAN (66 A.A.) Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL14 HUMAN (66 A.A.) Protein?
The endotoxin level is minimal, CCL14 HUMAN (66 A.A.) Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CST1 HumanDescription:
Cystatin SN Human Recombinant
Cystatin-SN, Cystain-SA-I, Cystatin-1, Salivary cystatin-SA-1, CST1.
Product # :
PRO-1006Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CST1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (21-141 a.a.) and having a molecular mass of 16.9kDa. CST1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CST1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Cystatin-SN (CST1) belongs to the type 2 salivary cystatin family found in a variety of fluids and secretions, including plasma, tears, and saliva. The cystatin superfamily includes proteins which contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, whereas others have lost or possibly never developed this inhibitory activity. CST1 is up-regulated in cancerous lesions of gastric cancer tissues compared to noncancerous regions, in addition clinicopathological analysis revealed a significant correlation between high expression of CST1.
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Synonyms
Cystatin-SN, Cystain-SA-I, Cystatin-1, Salivary cystatin-SA-1, CST1.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMWSPKEE DRIIPGGIYN ADLNDEWVQR ALHFAISEYN KATKDDYYRR PLRVLRARQQ TVGGVNYFFD VEVGRTICTK SQPNLDTCAF HEQPELQKKQ LCSFEIYEVP WENRRSLVKS RCQES.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.