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Search results

1000 results found for “prothymosin”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    STOM Human

    Description:

    Stomatin Human Recombinant

    BND7, EPB7, EPB72, Erythrocyte band 7 integral membrane protein, Protein 7.2b, Stomatin, STOM.

    Product # :

    PRO-1525

    Price :

    Quantity :

    Shipping Method :

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    • source
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    Description

    STOM Human Recombinant produced in E. coli is a single polypeptide chain containing 257 amino acids (55-288) and having a molecular mass of 28 kDa. STOM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The STOM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Stomatin (STOM) is a part of a highly conserved family of integral membrane proteins. STOM is a membrane protein involved in regulation of monovalent cation transport through lipid membranes which regulates ACCN1 and ACCN3 gating. STOM is a major lipid-raft component of erythrocytes and epithelial cells, and an abundant platelet protein which acts as a cytoskeletal anchor.

    • Synonyms

      BND7, EPB7, EPB72, Erythrocyte band 7 integral membrane protein, Protein 7.2b, Stomatin, STOM.

    • Physical Appearance

      Sterile Filtered clear 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSKIIKEYE RAIIFRLGRI LQGGAKGPGL FFILPCTDSF IKVDMRTISF DIPPQEILTK DSVTISVDGV VYYRVQNATL AVANITNADS ATRLLAQTTL RNVLGTKNLS QILSDREEIA HNMQSTLDDA TDAWGIKVER VEIKDVKLPV QLQRAMAAEA EASREARAKV IAAEGEMNAS RALKEASMVI TESPAALQLR YLQTLTTIAA EKNSTIVFPL PIDMLQGIIG AKHSHLG.

    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.

    Stom Human
  • View Data Sheet

    Name :

    SUMO3 Human

    Description:

    Small Ubiquitin-Related Modifier 3 Human Recombinant

    SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.

    Product # :

    PRO-267

    Price :

    Quantity :

    Shipping Method :

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    Description

    SUMO3 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 112 amino acids (1-92a.a.) and having a molecular mass of 12.6kDa (molecular weight on SDS-PAGE will appear higher).SUMO3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SUMO3 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl,1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SUMO3 belongs to the SUMO protein family and operates like ubiquitin. Nevertheless, unlike ubiquitin that targets proteins for degradation, SUMO3 protein takes part in several cellular processes, like nuclear transport, transcriptional regulation, apoptosis, and protein stability. SUMO3 regulates amyloid beta generation and is crucial in the onset or progression of Alzheimer’s disease.

    • Synonyms

      SUMO-3, SMT3A, SMT3H1, SMT3 homolog 1, Small Ubiquitin-related modifier 3, Ubiquitin-like protein SMT3A.

    • Physical Appearance

      Sterile Filtered clear 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSEEKPKEGV KTENDHINLK VAGQDGSVVQ FKIKRHTPLS KLMKAYCERQ GLSMRQIRFR FDGQPINETD TPAQLEMEDE DTIDVFQQQT GG

    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.

    Sumo3 Human
  • View Data Sheet

    Name :

    SYNJ2BP Human

    Description:

    Synaptojanin 2 Binding Protein Human Recombinant

    Synaptojanin 2 binding protein, ARIP2, OMP25, Synaptojanin-2-binding protein, Mitochondrial outer membrane protein 25, SYNJ2BP.

    Product # :

    PRO-1876

    Price :

    Quantity :

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    • Citations

    Description

    SYNJ2BP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-117 a.a) and having a molecular mass of 15.0kDa. SYNJ2BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SYNJ2BP protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Synaptojanin 2 Binding Protein (SYNJ2BP) contains 1 PDZ (DHR) domain which binds to isoform 2A of SYNJ2 (through the unique motif in the C-terminus) and interacts with MAPK12.

    • Synonyms

      Synaptojanin 2 binding protein, ARIP2, OMP25, Synaptojanin-2-binding protein, Mitochondrial outer membrane protein 25, SYNJ2BP.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMNGRVDY LVTEEEINLT RGPSGLGFNI VGGTDQQYVS NDSGIYVSRI KENGAAALDG RLQEGDKILS VNGQDLKNLL HQDAVDLFRN AGYAVSLRVQ HRLQVQNGPI GHRGEGDPSG.

    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.

    Synj2Bp Human
  • View Data Sheet

    Name :

    SYT3 Human

    Description:

    Synaptotagmin III Human Recombinant

    Synaptotagmin III, SYT3, SytIII, synaptotagmin-3.

    Product # :

    PRO-1937

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • Citations

    Description

    SYT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 540 amino acids (76-590) and having a molecular mass of 57.7 kDa.SYT3 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SYT3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Synaptotagmin-3 (SYT3) is a member of the synaptotagmin family. SYT3 is involved in Ca(2+)-dependent exocytosis of secretory vesicles through Ca(2+) and phospholipid binding to the C2 domain or may function as Ca(2+) sensors in the process of vesicular trafficking and exocytosis.

    • Synonyms

      Synaptotagmin III, SYT3, SytIII, synaptotagmin-3.

    • Physical Appearance

      Sterile Filtered clear 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEFWKLCW VPWRDKGGSA VGGGPLRKDL GPGVGLAGLV GGGGHHLAAG LGGHPLLGGP HHHAHAAHHP PFAELLEPGS LGGSDTPEPS YLDMDSYPEA AAAAVAAGVK PSQTSPELPS EGGAGSGLLL LPPSGGGLPS AQSHQQVTSL APTTRYPALP RPLTQQTLTS QPDPSSEERP PALPLPLPGG EEKAKLIGQI KPELYQGTGP GGRRSGGGPG SGEAGTGAPC GRISFALRYL YGSDQLVVRI LQALDLPAKD SNGFSDPYVK IYLLPDRKKK FQTKVHRKTL NPVFNETFQF SVPLAELAQR KLHFSVYDFD RFSRHDLIGQ VVLDNLLELA EQPPDRPLWR DIVEGGSEKA DLGELNFSLC YLPTAGRLTV TIIKASNLKA MDLTGFSDPY VKASLISEGR RLKKRKTSIK KNTLNPTYNE ALVFDVAPES VENVGLSIAV VDYDCIGHNE VIGVCRVGPD AADPHGREHW AEMLANPRKP VEHWHQLVEE KTVTSFTKGS KGLSEKENSE.

    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.

    Syt3 Human
  • View Data Sheet

    Name :

    CXCL8 Canine

    Description:

    Interleukin-8 Canine Recombinant

    Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8.

    Product # :

    CHM-009

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    Interleukin-8 Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 79 amino acids and having a molecular mass of 9.1kDa. The IL8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human CXCR2 transfected murine BaF3 cells is in a concentration range of 0.15-0.75 ng/ml.

    Citations

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL8 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.

    • Solubility

      It is recommended to reconstitute the lyophilized IL-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVLSRVSSEL RCQCIKTHST PFHPKYIKEL RVIDSGPHCE NSEIIVKLFN GNEVCLDPKE KWVQKVVQIF LKKAEKQDP.

    • Background

      What is the molecular weight/Mw of CXCL8 CANINE Protein?
      CXCL8 CANINE Protein has a total Mw of 9.1kDa.

      What is the source or expression system of CXCL8 CANINE Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 CANINE Protein?
      CXCL8 CANINE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 CANINE Protein?
      The biological activity determined by a chemotaxis bioassay using human CXCR2 transfected murine BaF3 cells is in a concentration range of 0.15-0.75 ng/ml.

      What is the amino acid sequence of CXCL8 CANINE Protein?
      AVLSRVSSEL RCQCIKTHST PFHPKYIKEL RVIDSGPHCE NSEIIVKLFN GNEVCLDPKE KWVQKVVQIF LKKAEKQDP.

      What applications can CXCL8 CANINE Protein be used in?
      CXCL8 CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 CANINE Protein?
      The endotoxin level is minimal, CXCL8 CANINE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL8 CANINE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL8 CANINE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Il 8 Canine
  • View Data Sheet

    Name :

    IL13RA2 Human

    Description:

    Interleukin 13 Receptor, Alpha 2 Human Recombinant

    CD213A2, CT19, IL-13R, IL13BP, IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, CD_antigen=CD213a2, Interleukin-13-binding protein.

    Product # :

    CYT-757

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    Description

    IL13RA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (27-343 a.a.) and having a molecular mass of 39.5kDa.IL13RA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL13RA2 protein solution (1mg/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.

    SDS-PAGE

    IL13RA2 Human - Product image 1

    Citations

    More Info

    • Introduction

      Interleukin 13 Receptor, Alpha 2 (IL13RA2) is a member of the type I cytokine receptor family, Type 5 subfamily. IL13RA2 is related to l13RA1, a subunit of the interleukin 13 receptor complex. IL13RA2 binds IL13 with high affinity, though lacking the cytoplasmic domain, and does not appear to function as a signal mediator. IL13RA2 plays a role in the internalization of IL13.

    • Synonyms

      CD213A2, CT19, IL-13R, IL13BP, IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, CD_antigen=CD213a2, Interleukin-13-binding protein.

    • Physical Appearance

      Sterile Filtered clear 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSDTEIKVN PPQDFEIVDP GYLGYLYLQW QPPLSLDHFK ECTVEYELKY RNIGSETWKT IITKNLHYKD GFDLNKGIEA KIHTLLPWQC TNGSEVQSSW AETTYWISPQ GIPETKVQDM DCVYYNWQYL LCSWKPGIGV LLDTNYNLFY WYEGLDHALQ CVDYIKADGQ NIGCRFPYLE ASDYKDFYIC VNGSSENKPI RSSYFTFQLQ NIVKPLPPVY LTFTRESSCE IKLKWSIPLG PIPARCFDYE IEIREDDTTL VTATVENETY TLKTTNETRQ LCFVVRSKVN IYCSDDGIWS EWSDKQCWEG EDLSKKTLLR.

    • Background

      What is the molecular weight/Mw of IL13RA2 HUMAN Protein?
      IL13RA2 HUMAN Protein has a total Mw of 39.5kDa.

      What is the source or expression system of IL13RA2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL13RA2 HUMAN Protein?
      IL13RA2 HUMAN Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL13RA2 HUMAN Protein?
      The biological functionality of IL13RA2 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IL13RA2 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSDTEIKVN PPQDFEIVDP GYLGYLYLQW QPPLSLDHFK ECTVEYELKY RNIGSETWKT IITKNLHYKD GFDLNKGIEA KIHTLLPWQC TNGSEVQSSW AETTYWISPQ GIPETKVQDM DCVYYNWQYL LCSWKPGIGV LLDTNYNLFY WYEGLDHALQ CVDYIKADGQ NIGCRFPYLE ASDYKDFYIC VNGSSENKPI RSSYFTFQLQ NIVKPLPPVY LTFTRESSCE IKLKWSIPLG PIPARCFDYE IEIREDDTTL VTATVENETY TLKTTNETRQ LCFVVRSKVN IYCSDDGIWS EWSDKQCWEG EDLSKKTLLR.

      What applications can IL13RA2 HUMAN Protein be used in?
      IL13RA2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL13RA2 HUMAN Protein?
      The endotoxin level is minimal, IL13RA2 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL13RA2 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL13RA2 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Il13Ra2 Human
  • View Data Sheet

    Name :

    FAS Human, His

    Description:

    sFas Receptor Human Recombinant, His Tag

    CD95, CD-95, Tumor necrosis factor receptor superfamily member 6, FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95 antigen, FAS, APT1, FAS1, TNFRSF6, APO-1, FASTM, ALPS1A.

    Product # :

    PRO-594

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    Description

    Recombinant FAS antigen/ CD95 purified from E. coli is a single non-glycosilated polypeptide chain containing amino acids 157-335 of Fas antigen. The recombinant CD95 is fused to C-terminal 6-histidine amino acids. The FAS antigen is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    10mM Sodium Phosphate, pH 8.0.

    Purity

    Greater than 95% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FAS / CD95 is a 36kDa transmembrane type I receptor, which belongs to the NF/NGF receptor super-family. It is a potent inducer of apoptosis in cells of the immune system upon interaction with its natural ligand, CD95L. Although the CD95/CD95L system could play a role in tumor regression, tumor cells seem to down-regulate CD95 expression as a mechanism of resistance to CD95L-induced killing by T lymphocytes and NK cells. The Fas antigen is expressed on the surface of various cell types, including activated T and B lymphocytes and T lymphoblastoid cell line. CD95 is also expressed in a broad panel of non-transformed cells outside the immune system.

    • Synonyms

      CD95, CD-95, Tumor necrosis factor receptor superfamily member 6, FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95 antigen, FAS, APT1, FAS1, TNFRSF6, APO-1, FASTM, ALPS1A.

    • Physical Appearance

      Sterile liquid formulation.

    • Stability

      CD95 although stable at 10°C for 5 days, should be stored below -18°C. Please prevent freeze-thaw cycles.

    • Background

      What is the source or expression system of FAS Protein?
      Escherichia Coli.

      What is the Purity of FAS Protein?
      FAS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FAS Protein?
      The biological functionality of FAS Protein will be determined in the future.

      What is the amino acid sequence of FAS Protein?
      FAS Protein is composed from 179 amino acids.

      What applications can FAS Protein be used in?
      FAS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FAS Protein?
      The endotoxin level is minimal, FAS 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.

    Cd95 Human His
  • View Data Sheet

    Name :

    PEBP1 Mouse

    Description:

    Phosphatidylethanolamine Binding Protein 1 Mouse Recombinant

    Phosphatidylethanolamine-binding protein 1, PEBP-1, HCNPpp.

    Product # :

    PRO-2230

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    Description

    PEBP1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187 a.a) and having a molecular mass of 23.2kDa. PEBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PEBP1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PEBP1 (Phosphatidylethanolamine binding protein 1) belongs to the phosphatidylethanolamine-binding protein family and a serine protease inhibitor that inhibits thrombin, neuropsin. PEBP1 plays a key modulatory part in several protein kinase signaling cascades. PKC phosphorylates PEBP1, resulting in the release of Raf-1 and activation of MEK and ERK. PEBP1 is expressed in many tissues and implicated in the regulation of such physiological processes as membrane biosynthesis, spermatogenesis, neural development, and metastasis suppression.
      PEBP1 binds ATP, opioids and phosphatidylethanolamine, however it has lower affinity for phosphatidylinositol and phosphatidylcholine. PEBP1 may also be involved in the function of the presynaptic cholinergic neurons of the CNS. PEBP1 increases the production of choline acetyltransferase although not acetylcholinesterase. Furtheremore, PEBP1 functions in potentially sequestering toxic compounds, including locostatin which may have harmful effects on cells.
      Loss of PEBP1 expression may have a significant role as prognostic marker in Gastrointestinal stromal tumors. In addition, PEBP1 is found differentially expressed in the Wernicke's Area from schizophrenia patients. PEBP1 is also, an invasion suppressor protein in nasopharyngeal carcinoma.

    • Synonyms

      Phosphatidylethanolamine-binding protein 1, PEBP-1, HCNPpp.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAADISQ WAGPLCLQEV DEPPQHALRV DYAGVTVDEL GKVLTPTQVM NRPSSISWDG LDPGKLYTLV LTDPDAPSRK DPKFREWHHF LVVNMKGNDI SSGTVLSDYV GSGPPSGTGL HRYVWLVYEQ EQPLSCDEPI LSNKSGDNRG KFKVETFRKK YNLGAPVAGT CYQAEWDDYV PKLYEQLSGK.

    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.

    Pebp1 Mouse
  • View Data Sheet

    Name :

    CALB2 Human

    Description:

    Calbindin-2 Human Recombinant

    Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.

    Product # :

    PRO-401

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    Description

    CALB2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1-271 a.a.) and having a molecular mass of 33.7kDa.The CALB2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CALB2 1mg/ml protein solution contains 20mM Tris-HCl buffer pH-8 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.

    • Synonyms

      Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSST EFMEAWRKYD TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL PVQENFLLKF QGMKLTSEEF NAIFTFYDKD RSGYIDEHEL DALLKDLYEK NKKEMNIQQL TNYRKSVMSL AEAGKLYRKD LEIVLCSEPP M.

    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.

    Calb2 Human
  • View Data Sheet

    Name :

    CXCL4 Mouse

    Description:

    Platelet Factor-4 Mouse Recombinant (CXCL4)

    CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    Product # :

    CHM-245

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    Description

    CXCL4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of 8.2kDa.

    Source

    Escherichia Coli.

    Formulation

    The Mouse CXCL4 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and 1.5M NaCl.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human neutrophils using a concentration range of 10-100ng/ml.

    Citations

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets. Its major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local activity and promoting coagulation. As a strong chemoattractant for neutrophils and fibroblasts, PF4 probably has a role in inflammation and wound repair. Oncostatin-A is a member of the CXC chemocinfamily.

    • Synonyms

      CXCL4, PF-4, PF4, Iroplact, Oncostatin-A, SCYB4, MGC138298.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized CXCL4 Mouse Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse CXCL4 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.

    • Solubility

      It is recommended to reconstitute the lyophilized CXCL4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VTSAGPEESD GDLSCVCVKT ISSGIHLKHI TSLEVIKAGR HCAVPQLIAT LKNGRKICLD RQAPLYKKVI KKILES.

    • Background

      What is the molecular weight/Mw of CXCL4 MOUSE Protein?
      CXCL4 MOUSE Protein has a total Mw of 8.2kDa.

      What is the source or expression system of CXCL4 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL4 MOUSE Protein?
      CXCL4 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL4 MOUSE Protein?
      Determined by its ability to chemoattract human neutrophils using a concentration range of 10-100ng/ml.

      What is the amino acid sequence of CXCL4 MOUSE Protein?
      VTSAGPEESD GDLSCVCVKT ISSGIHLKHI TSLEVIKAGR HCAVPQLIAT LKNGRKICLD RQAPLYKKVI KKILES.

      What applications can CXCL4 MOUSE Protein be used in?
      CXCL4 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL4 MOUSE Protein?
      The endotoxin level is minimal, CXCL4 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL4 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL4 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Platelet Factor 4 Mouse
  • View Data Sheet

    Name :

    FGF17 Human

    Description:

    Fibroblast Growth Factor 17 Human Recombinant

    Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    Product # :

    CYT-817

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    Description

    FGF17 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 22.6kDa.

    Source

    Escherichia Coli.

    Formulation

    FGF17 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.

    Citations

    More Info

    • Introduction

      Fibroblast Growth Factor 17 (FGF17) belongs to the fibroblast growth factor (FGF) family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes including embryonic development cell growth, morphogenesis, tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a role in central nervous system, bone and vascular development.

    • Synonyms

      Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF17 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.

    • Solubility

      It is recommended to reconstitute the lyophilized FGF17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.

    • Background

      What is the molecular weight/Mw of FGF17 Protein?
      FGF17 Protein has a total Mw of 22.6kDa.

      What is the source or expression system of FGF17 Protein?
      Escherichia Coli.

      What is the Purity of FGF17 Protein?
      FGF17 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF17 Protein?
      Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is less than 10 ng/ml, corresponding to a specific activity of >1.0 × 100,000 IU/mg.

      What is the amino acid sequence of FGF17 Protein?
      MTQGENHPSP NFNQYVRDQG AMTDQLSRRQ IREYQLYSRT SGKHVQVTGR RISATAEDGN KFAKLIVETD TFGSRVRIKG AESEKYICMN KRGKLIGKPS GKSKDCVFTE IVLENNYTAF QNARHEGWFM AFTRQGRPRQ ASRSRQNQRE AHFIKRLYQG QLPFPNHAEK QKQFEFVGSA PTRRTKRTRR PQPLT.

      What applications can FGF17 Protein be used in?
      FGF17 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF17 Protein?
      The endotoxin level is minimal, FGF17 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.

    Fgf 17 Human
  • View Data Sheet

    Name :

    FGF-18 Rat

    Description:

    Fibroblast Growth Factor-18 Rat Recombinant

    Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

    Product # :

    CYT-176

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    Description

    FGF18 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 21.0kDa.The FGF 18 Rat is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2um filtered concentrated solution in PBS and 0.5M NaCl, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×1,000,000 units/mg.

    sds-page

    FGF18 Rat sds-page - Product image 1

    Citations

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    • Introduction

      Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.

    • Synonyms

      Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF 18 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF 18 Rat 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 FGF 18 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQTELQK PFKYTTVTKR SRRIRPTHPG

    • Background

      What is the molecular weight/Mw of FGF18-RAT Protein?
      FGF18-RAT Protein has a total Mw of 21kDa.

      What is the source or expression system of FGF18-RAT Protein?
      Escherichia Coli.

      What is the Purity of FGF18-RAT Protein?
      FGF18-RAT Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF18-RAT Protein?
      The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×1,000,000 units/mg.

      What is the amino acid sequence of FGF18-RAT Protein?
      EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQTELQK PFKYTTVTKR SRRIRPTHPG

      What applications can FGF18-RAT Protein be used in?
      FGF18-RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF18-RAT Protein?
      The endotoxin level is minimal, FGF18-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.

    Fgf 18 Rat
  • View Data Sheet

    Name :

    PGM2 Human

    Description:

    Phosphoglucomutase 2 Human Recombinant

    Phosphoglucomutase 2, Glucose Phosphomutase 2, Phosphodeoxyribomutase, Phosphopentomutase, EC 5.4.2.2, PGM 2, Phosphoglucomutase-2, EC 5.4.2.7, EC 5.4.2, MSTP006.

    Product # :

    ENZ-930

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    Description

    PGM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 635 amino acids (1-612 a.a) and having a molecular mass of 70.7kDa. PGM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PGM2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PGM2 or Phosphoglucomutase-2 is a protein of the alpha-d-phosphohexomutase family that shares about 20% similarity with mammalian phosphoglucomutase 1. PGM2 Has low glucose 1,6-bisphosphate synthase activity. Furthermore, PGM2 catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. In addition, PGM2 catalyzes the interconversion of glucose-1-phosphate and glucose-6-phosphate.

    • Synonyms

      Phosphoglucomutase 2, Glucose Phosphomutase 2, Phosphodeoxyribomutase, Phosphopentomutase, EC 5.4.2.2, PGM 2, Phosphoglucomutase-2, EC 5.4.2.7, EC 5.4.2, MSTP006.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAAPEGS GLGEDARLDQ ETAQWLRWDK NSLTLEAVKR LIAEGNKEEL RKCFGARMEF GTAGLRAAMG PGISRMNDLT IIQTTQGFCR YLEKQFSDLK QKGIVISFDA RAHPSSGGSS RRFARLAATT FISQGIPVYL FSDITPTPFV PFTVSHLKLC AGIMITASHN PKQDNGYKVY WDNGAQIISP HDKGISQAIE ENLEPWPQAW DDSLIDSSPL LHNPSASINN DYFEDLKKYC FHRSVNRETK VKFVHTSVHG VGHSFVQSAF KAFDLVPPEA VPEQKDPDPE FPTVKYPNPE EGKGVLTLSF ALADKTKARI VLANDPDADR LAVAEKQDSG EWRVFSGNEL GALLGWWLFT SWKEKNQDRS ALKDTYMLSS TVSSKILRAI ALKEGFHFEE TLTGFKWMGN RAKQLIDQGK TVLFAFEEAI GYMCCPFVLD KDGVSAAVIS AELASFLATK NLSLSQQLKA IYVEYGYHIT KASYFICHDQ ETIKKLFENL RNYDGKNNYP KACGKFEISA IRDLTTGYDD SQPDKKAVLP TSKSSQMITF TFANGGVATM RTSGTEPKIK YYAELCAPPG NSDPEQLKKE LNELVSAIEE HFFQPQKYNL QPKAD.

    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.

    Pgm2 Human
  • View Data Sheet

    Name :

    CCL16 Human

    Description:

    LEC/NCC-4 Human Recombinant

    C-C motif chemokine 16, Small-inducible cytokine A16, IL-10-inducible chemokine, Chemokine LEC, Monotactin-1, Chemokine CC-4, Lymphocyte and monocyte chemoattractant, CCL-16, HCC-4, HCC4, NCC4, NCC-4, Liver Expressed Chemokine, LMC, LCC-1, LCC1, MTN-1, MTN1, SCYL4, ckB12, SCYA16, LEC, ILINCK, MGC117051.

    Product # :

    CHM-237

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    Description

    CCL16 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 97 amino acids and having a molecular mass of 11.2 kDa. The CCL16 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL16 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM PBS pH-7.4 and 0.15M sodium chloride.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract total human monocytes using a concentration range of 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    Citations

    More Info

    • Introduction

      Human CCL16, also called HCC-4, liver-expressed chemokine (LEC), and lymphocyte and monocyte chemoattractant (LMC), is a novel CC chemokine recognized by bioinformatics. NCC-4 cDNA encodes a 120 amino acids along with a 23 amino acids signal peptide that is cleaved to generate 97 amino acid protein. HCC4 is vaguely related to other CC chemokines, showing less than 30% sequence identity. Among CC chemokines, CCL-16 has the largest similarity to HCC-1. 2 potential polyadenylation signals are present on the human HCC-4 gene, and as a result, 2 transcripts containing roughly 1,500 base pairs and 500 base pairs have been detected. HCC-4 is expressed weakly by some lymphocytes, including NK cells, T cells, and some T cell clones. The expression of HCC-4 in monocytes is greatly upregulated in the presence of IL-10.
      CCL16 shows chemotactic activity for lymphocytes and monocytes rather than to neutrophils. NCC-4 has potent myelosuppressive activity, suppresses proliferation of myeloid progenitor cells. CCL16 demonstrates chemotactic activity for monocytes and thp-1 monocytes, rather than for resting lymphocytes and neutrophils. HCC-4 induces a calcium flux in thp-1 cells that desensitized prior to the expression of rantes.

    • Synonyms

      C-C motif chemokine 16, Small-inducible cytokine A16, IL-10-inducible chemokine, Chemokine LEC, Monotactin-1, Chemokine CC-4, Lymphocyte and monocyte chemoattractant, CCL-16, HCC-4, HCC4, NCC4, NCC-4, Liver Expressed Chemokine, LMC, LCC-1, LCC1, MTN-1, MTN1, SCYL4, ckB12, SCYA16, LEC, ILINCK, MGC117051.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL16 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL16 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.

    • Solubility

      It is recommended to reconstitute the lyophilized CCL16in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNP NDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ.

    • Background

      What is the molecular weight/Mw of CCL16 HUMAN Protein?
      CCL16 HUMAN Protein has a total Mw of 11.2kDa.

      What is the source or expression system of CCL16 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL16 HUMAN Protein?
      CCL16 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL16 HUMAN Protein?
      Determined by its ability to chemoattract total human monocytes using a concentration range of 10-100 ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL16 HUMAN Protein?
      QPKVPEWVNTPSTCCLKYYEKVLPRRLVVGYRKALNCHLPAIIFVTKRNREVCTNP NDDWVQEYIKDPNLPLLPTRNLSTVKIITAKNGQPQLLNSQ.

      What applications can CCL16 HUMAN Protein be used in?
      CCL16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL16 HUMAN Protein?
      The endotoxin level is minimal, CCL16 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL16 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL16 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Ccl16 Human
  • View Data Sheet

    Name :

    PHPT1 Human

    Description:

    Phosphohistidine Phosphatase 1 Human Recombinant

    PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.

    Product # :

    ENZ-012

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    Description

    PHPT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-125a.a.) and having a molecular mass of 15.9kDa.PHPT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHPT1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0) 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PHPT1 is a member of the Janus protein familyand is 125 amino acid long. PHPT1 appears as a monomer in the cytoplasm and is an EDTA-insensitive phosphohistidine phosphatase. Overexpression of PHPT1 resolts in specific phosphohistidine phosphatase activity towards phosphopeptide I, with no activity detected towards phosphotyrosine, phosphothreonine and phosphoserine peptides.

    • Synonyms

      PHP14, CGI-202, HSPC141, Phosphohistidine Phosphatase 1, Phosphohistidine Phosphatase 14kDa, Protein janus-A homolog, Sex-regulated protein Janus-a.

    • Physical Appearance

      Sterile Filtered clear 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAVADLALIP DVDIDSDGVF KYVLIRVHSA PRSGAPAAES KEIVRGYKWA EYHADIYDKV SGDMQKQGCD CECLGGGRIS HQSQDKKIHV YGYSMAYGPA QHAISTEKIK AKYPDYEVTW ANDGY

    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.

    Phpt1 Human
  • View Data Sheet

    Name :

    CXCL10 Mouse

    Description:

    IP-10 Mouse Recombinant (CXCL10)

    Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.

    Product # :

    CHM-336

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    • sds-page
    • Citations

    Description

    IP-10 Mouse Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8701 Dalton. The IP-10 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IP-10 was lyophilized from a 0.2µm filtered concentrated 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.

    Biological Activity

    Determined by its ability to chemoattract hCXCR3/HEK293 cells using a concentration range of 100.0-500.0 ng/ml.

    sds-page

    cxcl10 mouse sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family. CXCL10 is secreted by several cell types. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.

    • Synonyms

      Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IP-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL10 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.

    • Solubility

      It is recommended to reconstitute the lyophilized IP-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IPLARTVRCN CIHIDDGPVR MRAIGKLEII PASLSCPRVE IIATMKKNDE QRCLNPESKT IKNLMKAFSQ KRSKRAP.

    • Background

      What is the molecular weight/Mw of CXCL10 MOUSE Protein?
      CXCL10 MOUSE Protein has a total Mw of 8.7kDa.

      What is the source or expression system of CXCL10 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL10 MOUSE Protein?
      CXCL10 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL10 MOUSE Protein?
      Determined by its ability to chemoattract hCXCR3/HEK293 cells using a concentration range of 100.0-500.0 ng/ml.

      What is the amino acid sequence of CXCL10 MOUSE Protein?
      IPLARTVRCN CIHIDDGPVR MRAIGKLEII PASLSCPRVE IIATMKKNDE QRCLNPESKT IKNLMKAFSQ KRSKRAP.

      What applications can CXCL10 MOUSE Protein be used in?
      CXCL10 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL10 MOUSE Protein?
      The endotoxin level is minimal, CXCL10 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL10 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IP-10 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.

    Ip 10 Mouse
  • View Data Sheet

    Name :

    IRGM Human

    Description:

    Immunity-Related GTPase Family, M Human Recombinant

    Immunity-related GTPase family M protein, Immunity-related GTPase family M protein1, LPS-stimulated RAW 264.7 macrophage protein 47 homolog, LRG-47, IRGM, IFI1, IRGM1, LRG47.

    Product # :

    PRO-1302

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    Description

    IRGM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 180 amino acids (23-181) and having a molecular mass of 20.1 kDa. IRGM is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IRGM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Immunity-related GTPase family M protein (IRGM) is essential for clearance of severe protozoan and bacterial infections. IRGM belongs to the p47 immunity-related GTPase family. IRGM serves in innate immune response possibly via regulation of autophagy. IRGM regulates proinflammatory cytokine production and inhibit endotoxemia upon infection and also has a part in macrophages adhesion and motility. Polymorphisms which modify the natural expression of the IRGM gene are associated with a susceptibility to Crohn's disease and tuberculosis.

    • Synonyms

      Immunity-related GTPase family M protein, Immunity-related GTPase family M protein1, LPS-stimulated RAW 264.7 macrophage protein 47 homolog, LRG-47, IRGM, IFI1, IRGM1, LRG47.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKETLKIVSR TPVNITMAGD SGNGMSTFIS ALRNTGHEGK ASPPTELVKA TQRCASYFSS HFSNVVLWDL PGTGSATTTL ENYLMEMQFN RYDFIMVASA QFSMNHVMLA KTAEDMGKKF YIVWTKLDMD LSTGALPEVQ LLQIRENVLE NLQKERVCEY.

    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.

    Irgm Human
  • View Data Sheet

    Name :

    JOSD1 Human

    Description:

    Josephin Domain Containing 1 Human Recombinant

    Josephin-1, Josephin domain-containing 1, JOSD1, JSPH1, KIAA0063, dJ508I15.2.

    Product # :

    PRO-1251

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    Description

    JOSD1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-202 a.a.) and having a molecular mass of 25.6kDa.JOSD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    JOSD1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol, 5mM DTT and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Josephin-1 (JOSD1) has minimal protease activity towards poly-ubiquitin chains (in vitro). JOSD1 functions as a deubiquitinating enzyme. Ubiquitin-binding sites in the Josephin domain are a factor in ubiquitin chain binding and cleavage.

    • Synonyms

      Josephin-1, Josephin domain-containing 1, JOSD1, JSPH1, KIAA0063, dJ508I15.2.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSCVPWK GDKAKSESLE LPQAAPPQIY HEKQRRELCA LHALNNVFQD SNAFTRDTLQ EIFQRLSPNT MVTPHKKSML GNGNYDVNVI MAALQTKGYE AVWWDKRRDV GVIALTNVMG FIMNLPSSLC WGPLKLPLKR QHWICVREVG GAYYNLDSKL KMPEWIGGES ELRKFLKHHL RGKNCELLLV VPEEVEAHQS WRTDV.

    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.

    Josd1 Human
  • View Data Sheet

    Name :

    TMIGD2 Human

    Description:

    Transmembrane And Immunoglobulin Domain Containing 2 Human Recombinant

    IGPR-1, IGPR1,TMIGD2, Transmembrane and immunoglobulin domain-containing protein 2 isoform1, CD28 homolog, CD28H, Immunoglobulin and proline-rich receptor 1.

    Product # :

    PRO-2808

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    Description

    TMIGD2 Human Recombinant is a single, glycosylated, polypeptide chain (23-150 a.a) containing a total of 361 amino acids and having a molecular mass of 40.1 kDa. TMIGD2 is fused to a 233 a.a hIgG -Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The TMIGD2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range is ≤ 200 ng/ml and is measured by its binding ability in a functional ELISA with Human HHLA2.

    Citations

    More Info

    • Synonyms

      IGPR-1, IGPR1,TMIGD2, Transmembrane and immunoglobulin domain-containing protein 2 isoform1, CD28 homolog, CD28H, Immunoglobulin and proline-rich receptor 1.

    • 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.

    • Amino Acid Sequence

      LSVQQGPNLL QVRQGSQATL VCQVDQATAW ERLRVKWTKD GAILCQPYIT NGSLSLGVCG PQGRLSWQAP SHLTLQLDPV SLNHSGAYVC WAAVEIPELE EAEGNITRLF VDPDDPTQNR NRIASFPGLE PKSCDKTHTC PPCPAPELLG GPSVFLFPPK PKDTLMISRT PEVTCVVVDV SHEDPEVKFN WYVDGVEVHN AKTKPREEQY NSTYRVVSVL TVLHQDWLNG KEYKCKVSNK ALPAPIEKTI SKAKGQPREP QVYTLPPSRD ELTKNQVSLT CLVKGFYPSD IAVEWESNGQ PENNYKTTPP VLDSDGSFFL YSKLTVDKSR WQQGNVFSCS VMHEALHNHY TQKSLSLSPGK.

    • Background

      TMIGD2 in Autoimmune Disorders:

      Conversely, dysregulation of TMIGD2 may contribute to autoimmune disorders, where the immune system mistakenly targets the body's own tissues. Investigations into TMIGD2 Human Recombinant may shed light on its role in immune tolerance and the prevention of excessive immune reactions. Deciphering the nuances of TMIGD2's functions provides potential insights for therapeutic interventions in autoimmune conditions.

      Challenges and Future Directions:

      While the potential of TMIGD2 Human Recombinant in immune modulation is promising, challenges persist. Fine-tuning its applications, understanding its interactions with various immune cell types, and deciphering the context-dependent nature of its functions are critical considerations for translational success. Additionally, exploring the potential dual role of TMIGD2 in cancer immunity and autoimmune disorders poses a challenge in the pursuit of targeted therapeutic strategies.

      TMIGD2 Human Recombinant emerges as a promising protagonist in the narrative of immune modulation, offering a controlled platform for scientific exploration. Its structural insights, cellular functions, and implications in immune regulation position it as a key player in the evolving landscape of immunotherapy and immune-related disorders. As researchers continue to unravel the molecular intricacies of TMIGD2, they not only deepen our understanding of immune responses but also pave the way for transformative advancements in cancer immunotherapy and autoimmune disease therapeutics, shaping the future of precision medicine and immunomodulatory interventions.

    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.

    Tmigd2 Human
  • View Data Sheet

    Name :

    KARS Human

    Description:

    Lysyl-tRNA Synthetase Human Recombinant

    Lysine--tRNA ligase, Lysyl-tRNA synthetase, LysRS, KARS, KIAA0070, KRS, KARS2, CMTRIB.

    Product # :

    ENZ-161

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    Description

    KARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 558 amino acids (63-597 a.a.) and having a molecular mass of 63.7kDa.KARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KARS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lysyl-tRNA synthetase (KARS) is a member of the class-II aminoacyl-tRNA synthetase family. KARS exists as both mitochondrial and cytoplasmic isoforms produced by alternative splicing, and believed to have a role in autoimmune diseases, such as polymyositis or dermatomyositis. The KARS protein functions to catalyze the aminoacylation of tRNAs by their corresponding amino acids, so linking amino acids with tRNA-contained nucleotide triplets.

    • Synonyms

      Lysine--tRNA ligase, Lysyl-tRNA synthetase, LysRS, KARS, KIAA0070, KRS, KARS2, CMTRIB.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSGVGPEEE SVDPNQYYKI RSQAIHQLKV NGEDPYPHKF HVDISLTDFI QKYSHLQPGD HLTDITLKVA GRIHAKRASG GKLIFYDLRG EGVKLQVMAN SRNYKSEEEF IHINNKLRRG DIIGVQGNPG KTKKGELSII PYEITLLSPC LHMLPHLHFG LKDKETRYRQ RYLDLILNDF VRQKFIIRSK IITYIRSFLD ELGFLEIETP MMNIIPGGAV AKPFITYHNE LDMNLYMRIA PELYHKMLVV GGIDRVYEIG RQFRNEGIDL THNPEFTTCE FYMAYADYHD LMEITEKMVS GMVKHITGSY KVTYHPDGPE GQAYDVDFTP PFRRINMVEE LEKALGMKLP ETNLFETEET RKILDDICVA KAVECPPPRT TARLLDKLVG EFLEVTCINP TFICDHPQIM SPLAKWHRSK EGLTERFELF VMKKEICNAY TELNDPMRQR QLFEEQAKAK AAGDDEAMFI DENFCTALEY GLPPTAGWGM GIDRVAMFLT DSNNIKEVLL FPAMKPEDKK ENVATTDTLE STTVGTSV.

    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.

    Kars Human
  • View Data Sheet

    Name :

    Placental Lactogen Ovine

    Description:

    Placental Lactogen Ovine Recombinant

    Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    Product # :

    CYT-512

    Price :

    Quantity :

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    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info
    • Citations

    Description

    Placental Lactogen Ovine Recombinant, is a single polypeptide chain containing 199 amino acids and an additional Ala at the N-terminus having a molecular mass of 23 kDa. Placental Lactogen Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis gel filtration.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Placental Lactogen Ovine is biologically active as evidenced by inducing proliferation of Nb2 cells.

    Citations

    More Info

    • Introduction

      Placental Lactogen is a polypeptide hormone that is produced by the Syncytiotrophoblasts of the Placenta, also known as chorionic somatomammotropin. It has both Growth Hormone and Prolactin activities on growth, lactation, and luteal steroid production. In women, placental lactogen secretion begins soon after implantation and increases to 1 g or more a day in late pregnancy. Placental lactogen is also an insulin antagonist.
      Placental Lactogen Ovine is also capable of activating human and other heterologous GH receptors but not ruminat GH receptors.

    • Synonyms

      Chorionic Somatomammotropin Hormone 1, CSH1, CS-1, hCS, PL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Placental Lactogen Ovine Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Placental Lactogen 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Placental Lactogen in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Gln-His-Pro-Pro.

    • Protein content

      UV spectroscopy at 280 nm using the absorbency value of 0.85 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Placental Lactogen Ovine
  • View Data Sheet

    Name :

    PMF1-BGLAP Human

    Description:

    PMF1-BGLAP Human Recombinant

    PMF1-BGLAP Readthrough, PMF1-BGLAP Protein, Polyamine-Modulated Factor 1, PMF1.

    Product # :

    PRO-1760

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    Description

    PMF1-BGLAP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 234 amino acids (1-211aa) and having a molecular mass of 26.2kDa.PMF1-BGLAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PMF1-BGLAP 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.

    Citations

    More Info

    • Introduction

      PMF1-BGLAP is a locus which represents naturally occurring read-through transcription between the neighboring polyamine-modulated factor 1 (PMF1) and bone gamma-carboxyglutamate Gla protein (BGLAP) genes on chromosome 1. There are multiple transcript variants encoding isoforms as a results of alternative splicing which share sequence identity with the upstream gene product, but they have a different C-termini because of frameshifts as opposed to the downstream gene coding sequence.

    • Synonyms

      PMF1-BGLAP Readthrough, PMF1-BGLAP Protein, Polyamine-Modulated Factor 1, PMF1.

    • Physical Appearance

      Sterile Filtered clear 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAEASSA NLGSGCEEKR HEGSSSESVP PGTTISRVKL LDTMVDTFLQ KLVAAGSYQR FTDCYKCFYQ LQPAMTQQIY DKFIAQLQTS IREEISDIKE EGNLEAVLNA LDKIVEEGKV RKEPAWRPSG IPEKDLHSVM APYFLQQRDT LRRHVQKQEA ENQQLADAVL AGRRQVEELQ LQVQAQQQAW QVRSPAVQSP AKVQPLCPSR RAAR

    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.

    Pmf1 Bglap Human
  • View Data Sheet

    Name :

    PMVK Human

    Description:

    Phosphomevalonate Kinase Human Recombinant

    Phosphomevalonate kinase, PMKase, hPMK, PMVK, PMKI, PMK, PMKA, PMKASE, HUMPMKI.

    Product # :

    PKA-308

    Price :

    Quantity :

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    • source
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    Description

    PMVK Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 212 amino acids (1-192 a.a.) and having a molecular mass of 24.1kDa. The PMVK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PMVK solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Phosphomevalonate kinase (PMVK) is a cytosolic enzyme. PMVK is expressed highly in the heart, liver, skeletal muscle, kidney and pancreas and slightly lower in the brain, placenta, and lung. PMVK catalyzes the conversion of mevalonate 5-phosphate into mevalonate 5-diphosphate in the fifth reaction of the cholesterol biosynthetic pathway. Induced by sterol, PMVK participates in isopentenyl diphosphate biosynthesis via the mevalonate pathway.

    • Synonyms

      Phosphomevalonate kinase, PMKase, hPMK, PMVK, PMKI, PMK, PMKA, PMKASE, HUMPMKI.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAPLGGAPRL VLLFSGKRKS GKDFVTEALQ SRLGADVCAV LRLSGPLKEQ YAQEHGLNFQ RLLDTSTYKE AFRKDMIRWG EEKRQADPGF FCRKIVEGIS QPIWLVSDTR RVSDIQWFRE AYGAVTQTVR VVALEQSRQQ RGWVFTPGVD DAESECGLDN FGDFDWVIEN HGVEQRLEEQ LENLIEFIRS RL.

    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.

    Pmvk Human
  • View Data Sheet

    Name :

    TOR1A Human

    Description:

    Torsin Family 1 Member A Human Recombinant

    DQ2, DYT1, Torsin-1A, Dystonia 1 protein, Torsin family 1 member A, TOR1A.

    Product # :

    PRO-1430

    Price :

    Quantity :

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    Description

    TOR1A Human Recombinant produced in E. coli is a single polypeptide chain containing 333 amino acids (21-332) and having a molecular mass of 38kDa. TOR1A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TOR1A solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      TOR1A which is a member of the AAA family of adenosine triphosphatases (ATPases) is associated to the Clp protease/heat shock family and is expressed highly in the substantia nigra pars compacta.TOR1A functions as a molecular chaperone assisting in the suitable folding of secreted and/or membrane proteins. Mutations in TOR1A result in the autosomal dominant disorder, torsion dystonia one.

    • Synonyms

      DQ2, DYT1, Torsin-1A, Dystonia 1 protein, Torsin family 1 member A, TOR1A.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MVEPISLGLA LAGVLTGYIY PRLYCLFAEC CGQKRSLSRE ALQKDLDDNL FGQHLAKKII LNAVFGFINN PKPKKPLTLS LHGWTGTGKN FVSKIIAENI YEGGLNSDYV HLFVATLHFP HASNITLYKD QLQLWIRGNV SACARSIFIF DEMDKMHAGL IDAIKPFLDY YDLVDGVSYQ KAMFIFLSNA GAERITDVAL DFWRSGKQRE DIKLKDIEHA LSVSVFNNKN SGFWHSSLIH RNLIDYFVPF LPLEYKHLKM CIRVEMQSRG YEIDEDIVSR VAEEMTFFPK EERVFSDKGC KTVFTKLDYY YDD.

    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.

    Tor1A Human
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