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Search results

1000 results found for “cyclin”

Name

Description

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  • View Data Sheet

    Name :

    CEA Human, His

    Description:

    Carcinoembryonic Antigen Human Recombinant, His Tag

    Carcinoembryonic Antigen Related Cell Adhesion Molecule 5, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 5, Meconium Antigen 100, CEA, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic antigen-related cell adhesion molecule 5, Carcinoembryonic antigen, CEA.

    Product # :

    PRO-2407

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    Description

    CEA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 659 amino acids (35-685a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-150kDa). CEA is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CEA protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
      There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
      The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
      CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
      The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
      Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed.

    • Synonyms

      Carcinoembryonic Antigen Related Cell Adhesion Molecule 5, Carcinoembryonic Antigen-Related Cell Adhesion Molecule 5, Meconium Antigen 100, CEA, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic antigen-related cell adhesion molecule 5, Carcinoembryonic antigen, CEA.

    • 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

      KLTIESTPFN VAEGKEVLLL VHNLPQHLFG YSWYKGERVD GNRQIIGYVI GTQQATPGPA YSGREIIYPN ASLLIQNIIQ NDTGFYTLHV IKSDLVNEEA TGQFRVYPEL PKPSISSNNS KPVEDKDAVA FTCEPETQDA TYLWWVNNQS LPVSPRLQLS NGNRTLTLFN VTRNDTASYK CETQNPVSAR RSDSVILNVL YGPDAPTISP LNTSYRSGEN LNLSCHAASN PPAQYSWFVN GTFQQSTQEL FIPNITVNNS GSYTCQAHNS DTGLNRTTVT TITVYAEPPK PFITSNNSNP VEDEDAVALT CEPEIQNTTY LWWVNNQSLP VSPRLQLSND NRTLTLLSVT RNDVGPYECG IQNKLSVDHS DPVILNVLYG PDDPTISPSY TYYRPGVNLS LSCHAASNPP AQYSWLIDGN IQQHTQELFI SNITEKNSGL YTCQANNSAS GHSRTTVKTI TVSAELPKPS ISSNNSKPVE DKDAVAFTCE PEAQNTTYLW WVNGQSLPVS PRLQLSNGNR TLTLFNVTRN DARAYVCGIQ NSVSANRSDP VTLDVLYGPD TPIISPPDSS YLSGANLNLS CHSASNPSPQ YSWRINGIPQ QHTQVLFIAK ITPNNNGTYA CFVSNLATGR NNSIVKSITV SASGTSPGLS ALEHHHHHH.

    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.

    Ceacam5 Human
  • View Data Sheet

    Name :

    Fertirelin

    Description:

    Fertirelin

    Product # :

    HOR-037

    Price :

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    Description

    Fertirelin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1153.31 Dalton and a Molecular formula of C55H76N16O12.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-NHEt.

    • Background

      Fertirelin, a potent gonadotropin-releasing hormone (GnRH) analogue, is crucial for fertility regulation in animals. This research paper endeavors to expound on the biochemical attributes of fertirelin and its potential therapeutic applications in veterinary medicine.

      Fertirelin, a synthetic analogue of the natural gonadotropin-releasing hormone, plays a fundamental role in fertility regulation in veterinary medicine. It stimulates the secretion of luteinizing hormone and follicle-stimulating hormone, crucial for reproduction (Kotwica et al., 2005). This paper aims to delve into the biochemical characteristics of fertirelin and its potential applications.

      Fertirelin, as a GnRH analogue, elicits its action by binding to GnRH receptors located on pituitary gonadotroph cells. This leads to the release of luteinizing hormone and follicle-stimulating hormone, key players in ovulation and spermatogenesis (Kotwica et al., 2005).

      In the realm of veterinary medicine, fertirelin is primarily used for treating ovarian follicular cysts in dairy cattle (Bosu & Peter, 1987). Its potent stimulatory effect on gonadotropin secretion facilitates ovulation and contributes to fertility management strategies.

      The potential of fertirelin extends beyond the current applications. Further research into the precise mechanism of action and potential side effects can enhance its utilization. Overall, fertirelin presents a powerful tool in veterinary reproductive medicine, making it a focal point of interest for future studies.

    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.

    Fertirelin
  • View Data Sheet

    Name :

    DBNDD2 Human

    Description:

    Dysbindin (Dystrobrevin Binding Protein 1) Domain Containing 2 Human Recombinant

    Dysbindin domain-containing protein 2, Casein kinase-1 binding protein, CK1BP, HSMNP1, DBNDD2, C20orf35.

    Product # :

    PRO-1167

    Price :

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    Description

    DBNDD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (1-161 a.a) and having a molecular mass of 20.1kDa (Molecular weight on SDS-PAGE will appear higher).DBNDD2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DBNDD2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dysbindin domain-containing protein 2 (DBNDD2) is a member of the dysbindin family. DBNDD2 regulates the activity of casein kinase-1 and inhibits CSNK1D autophosphorylation (in vitro). DBNDD2 also interacts with CSNK1D and CSNK1E. DBNDD2 is detected in brain.

    • Synonyms

      Dysbindin domain-containing protein 2, Casein kinase-1 binding protein, CK1BP, HSMNP1, DBNDD2, C20orf35.

    • 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 MGSHMDPNPR AALERQQLRL RERQKFFEDI LQPETEFVFP LSHLHLESQR PPIGSISSME VNVDTLEQVE LIDLGDPDAA DVFLPCEDPP PTPQSSGMDN HLEELSLPVP TSDRTTSRTS SSSSSDSSTN LHSPNPSDDG ADTPLAQSDE EEERGDGGAE PGACS.

    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.

    Dbndd2 Human
  • View Data Sheet

    Name :

    Noggin Human, Sf9

    Description:

    Noggin Human Recombinant, Sf9

    SYM1, SYNS1, NOG.

    Product # :

    CYT-1119

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
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    • biological activity
    • More Info

    Description

    Noggin produced in Sf9 Baculovirus cells is a glycosylated homodimer containing 205 amino acids and having a molecular mass of 47.9kDa under non-reducing conditions. (Molecular size on SDS-PAGE will appear at approximately 50-80kDa).Noggin is purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20 and 5% trehalose.

    Purity

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

    Biological Activity

    Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cellsans was fount to be 0.04‑0.2 μg/mL in the presence of 50 ng/mL of Recombinant Human BMP‑4.

    More Info

    • Introduction

      Nogginwhich is encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may play and important role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. Noggin was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. There are several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1). All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

    • Synonyms

      SYM1, SYNS1, NOG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC.

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    Noggin Protein
  • View Data Sheet

    Name :

    NOV Human, HEK

    Description:

    Nephroblastoma Overexpressed Human Recombinant, HEK

    Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    Product # :

    CYT-1032

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    Description

    NOV Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 33-357) containing 331 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 36.5kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    NOV filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.

    • Synonyms

      Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • 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 one week at 4°C.

    • 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. NOV is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      QRCPPQCPGR CPATPPTCAP GVRAVLDGCS CCLVCARQRG ESCSDLEPCD ESSGLYCDRS ADPSNQTGIC TAVEGDNCVF DGVIYRSGEK FQPSCKFQCT CRDGQIGCVP RCQLDVLLPE PNCPAPRKVE VPGECCEKWI CGPDEEDSLG GLTLAAYRPE ATLGVEVSDS SVNCIEQTTE WTACSKSCGM GFSTRVTNRN RQCEMLKQTR LCMVRPCEQE PEQPTDKKGK KCLRTKKSLK AIHLQFKNCT SLHTYKPRFC GVCSDGRCCT PHNTKTIQAE FQCSPGQIVK KPVMVIGTCT CHTNCPKNNE AFLQELELKT TRGKMHHHHH H.

    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.

    Nov Protein
  • View Data Sheet

    Name :

    PDCD6 Human

    Description:

    Programmed Cell Death 6 Human Recombinant

    Programmed cell death 6, ALG-2, PEF1B, Apoptosis-linked gene 2 protein, Probable calcium-binding protein ALG-2, FLJ46208, MGC111017, MGC119050, MGC9123.

    Product # :

    PRO-184

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    Description

    PDCD6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (1-191a.a.) and having a molecular mass of 24.0 kDa. PDCD6 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PDCD6 protein solution (0.5mg/1ml) is formulated in 10mM sodium citrate (pH 3.5) and 40% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PDCD6 is a calcium-binding protein and is a member of the penta-EF-hand protein family. Calcium binding is vital for homodimerization and for conformational changes essential for binding to other protein partners. PDCD6 takes part in T cell receptor-, Fas-, and glucocorticoid-induced programmed cell death. However, tests showed that in mice deficient for PDCD6, apoptosis was not blocked which suggests that PDCD6 is functionally redundant.

    • Synonyms

      Programmed cell death 6, ALG-2, PEF1B, Apoptosis-linked gene 2 protein, Probable calcium-binding protein ALG-2, FLJ46208, MGC111017, MGC119050, MGC9123.

    • 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 MAAYSYRPGP GAGPGPAAGA ALPDQSFLWN VFQRVDKDRS GVISDTELQQ ALSNGTWTPF NPVTVRSIIS MFDRENKAGV NFSEFTGVWK YITDWQNVFR TYDRDNSGMI DKNELKQALS GFGYRLSDQF HDILIRKFDR QGRGQIAFDD FIQGCIVLQR LTDIFRRYDT DQDGWIQVSY EQYLSMVFSI V

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    Pdcd6 Human
  • View Data Sheet

    Name :

    HAVCR1 Human, HEK

    Description:

    Hepatitis A Virus Cellular Receptor 1 Human Recombinant, HEK

    Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.

    Product # :

    HAV-223

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    Description

    HAVCR1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Ser21-Thr288) containing a total of 283 amino acids, having a calculated molecular mass of 30.5kDa. HAVCR1 is fused to a 2 aa N-terminal linker, a 2 aa C-terminal linker and a 6 aa His tag at C-Terminus.

    Source

    HEK 293.

    Formulation

    HAVCR1 was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% (w/v) Trehalose.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hepatitis A virus cellular receptor 1 (HAVCR1) is a membrane receptor for both human hepatitis A virus (HHAV) and TIMD4. HAVCR1 is a type I trans-membrane structural glycoprotein located in the renal proximal tubule epithelial cells. HAVCR1 protein may be involved in the control of asthma and allergic diseases. The reference genome represents an allele which retains a MTTVP amino acid segment that presents defense against atopy in HHAV seropositive individuals.

    • Synonyms

      Hepatitis A Virus Cellular Receptor 1, T-Cell Immunoglobulin Mucin Family Member 1, T-Cell Immunoglobulin Mucin Receptor 1, T-Cell Membrane Protein 1, Kidney Injury Molecule 1, HAVCR-1, TIMD-1, HAVCR, KIM-1, TIM-1, TIMD1, TIM1, KIM1, TIM, T-Cell Immunoglobulin And Mucin Domain-Containing Protein 1, T Cell Immunoglobin Domain And Mucin Domain Protein 1, HAVCR1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. HAVCR1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      ASSVKVGGEA GPSVTLPCHY SGAVTSMCWN RGSCSLFTCQ NGIVWTNGTH VTYRKDTRYK LLGDLSRRDV SLTIENTAVS DSGVYCCRVE HRGWFNDMKI TVSLEIVPPK VTTTPIVTTV PTVTTVRTST TVPTTTTVPM TTVPTTTVPT TMSIPTTTTV LTTMTVSTTT SVPTTTSIPT TTSVPVTTTV STFVPPMPLP RQNHEPVATS PSSPQPAETH PTTLQGAIRR EPTSSPLYSY TTDGNDTVTE SSDGLWNNNQ TQLFLEHSLL TANTTKLHHH HHH.

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    Havcr1 Human Hek
  • View Data Sheet

    Name :

    MED27 Human

    Description:

    Mediator Complex Subunit 27 Human Recombinant

    Mediator Complex Subunit 27, MED27, CRSP8, Cofactor Required For Sp1 Transcriptional Activation, Subunit 8 34kDa, P37 TRAP/SMCC/PC2 Subunit, Transcriptional Coactivator CRSP34, CRSP34, CRSP Complex Subunit 8, CRAP34, TRAP37, Mediator of RNA Polymerase II Transcription Subunit 27, Cofactor Required For Sp1 Transcriptional Activation Subunit 8.

    Product # :

    PRO-1946

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    Description

    MED27 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-311) and having a molecular mass of 37.8 kDa.MED27 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MED27 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mediator Complex Subunit 27 (MED27) is a subunit of the CRSP (cofactor required for SP1 activation) complex, which, together with TFIID, is necessary for efficient activation by SP1. MED27 is a component of the Mediator complex, a coactivator involved in the regulated transcription of virtually all RNA polymerase II-dependent genes. MED27 protein is also a component of other multisubunit complexes such as the thyroid hormone receptor-(TR-) associated proteins which interact with TR and facilitate TR function on DNA templates in conjunction with initiation factors and cofactors. The activation of MED27 gene transcription is a multistep process, which is triggered by factors that identify transcriptional enhancer sites in DNA.

    • Synonyms

      Mediator Complex Subunit 27, MED27, CRSP8, Cofactor Required For Sp1 Transcriptional Activation, Subunit 8 34kDa, P37 TRAP/SMCC/PC2 Subunit, Transcriptional Coactivator CRSP34, CRSP34, CRSP Complex Subunit 8, CRAP34, TRAP37, Mediator of RNA Polymerase II Transcription Subunit 27, Cofactor Required For Sp1 Transcriptional Activation Subunit 8.

    • 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 MGSMADVINV SVNLEAFSQA ISAIQALRSS VSRVFDCLKD GMRNKETLEG REKAFIAHFQ DNLHSVNRDL NELERLSNLV GKPSENHPLH NSGLLSLDPV QDKTPLYSQL LQAYKWSNKL QYHAGLASGL LNQQSLKRSA NQMGVSAKRR PKAQPTTLVL PPQYVDDVIS RIDRMFPEMS IHLSRPNGTS AMLLVTLGKV LKVIVVMRSL FIDRTIVKGY NENVYTEDGK LDIWSKSNYQ VFQKVTDHAT TALLHYQLPQ MPDVVVRSFM TWLRSYIKLF QAPCQRCGKF LQDGLPPTWR DFRTLEAFHD TCRQ.

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    Med27 Human
  • View Data Sheet

    Name :

    CSTB Human

    Description:

    Cystatin B Human Recombinant

    Cystatin-B, Stefin-B, Liver thiol proteinase inhibitor, CPI-B, CSTB, CST6, EPM1, PME, STFB.

    Product # :

    PRO-609

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    Description

    CSTB Human Recombinant fused to a 20 a.a His-Tag at N-Terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-98 a.a) and having a molecular mass of 13 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH-8 & 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Type 1 cystatins are also called stefins which function as intracellular thiol protease inhibitors. Cystatin-B protein is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. CSTB protein protects proteases leakage from lysosomes. Mutations in Stefin-B gene cause primary defects in patients with progressive myoclonic epilepsy (EPM1), a degenerative disease of the central nervous system. CSTB is overexpressed & elevated in the serum of HCC patients. Cystatin-B in vivo has a polymeric structure which is sensitive to the redox environment. Cystatin-B inhibits bone resorption by down-regulating intracellular cathepsin K activity despite increased osteoclast survival. Protein and mRNA levels of stefin B are significantly lower in atypical benign meningiomas. Stefins-A & Stefin-B which belong to the type-1 Cystatins, are up-regulated in lung tumours and thus able to counteract harmful tumour-associated proteolytic activity. Human stefin-A & Stefin-B form amyloid fibrils. Copper binding by stefin-B reduces amyloid fibril formation. A number of alternatively spliced CSTB isoforms were recognized in patients with progressive myoclonus epilepsy. Decreased CSTB activity in EPM1 pathogenesis is controled by cathepsins through increased activity of cathepsin-S & cathepsin-L.

    • Synonyms

      Cystatin-B, Stefin-B, Liver thiol proteinase inhibitor, CPI-B, CSTB, CST6, EPM1, PME, STFB.

    • 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 MMCGAPSATQ PATAETQHIA DQVRSQLEEK ENKKFPVFKA VSFKSQVVAG TNYFIKVHVG DEDFVHLRVF QSLPHENKPL TLSNYQTNKA KHDELTYF.

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    Cystatin B Human
  • View Data Sheet

    Name :

    CUEDC2 Human

    Description:

    CUE Domain Containing 2 Human Recombinant

    CUE domain-containing protein 2, CUEDC2, C10orf66, HOYS6, bA18I14.5.

    Product # :

    PRO-1680

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    Description

    CUEDC2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-287) and having a molecular mass of 34 kDa.CUEDC2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CUEDC2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CUE Domain Containing 2 also known as CUEDC2 is a part of the CUEDC2 family and contains 1 CUE domain. CUEDC2 down-regulates ESR1 protein levels through the ubiquitination-proteasome pathway and controls PGR protein levels through a parallel mechanism.

    • Synonyms

      CUE domain-containing protein 2, CUEDC2, C10orf66, HOYS6, bA18I14.5.

    • 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 MGSMELERIV SAALLAFVQT HLPEADLSGL DEVIFSYVLG VLEDLGPSGP SEENFDMEAF TEMMEAYVPG FAHIPRGTIG DMMQKLSGQL SDARNKENLQ PQSSGVQGQV PISPEPLQRP EMLKEETRSS AAAAADTQDE ATGAEEELLP GVDVLLEVFP TCSVEQAQWV LAKARGDLEE AVQMLVEGKE EGPAAWEGPN QDLPRRLRGP QKDELKSFIL QKYMMVDSAE DQKIHRPMAP KEAPKKLIRY IDNQVVSTKG ERFKDVRNPE AEEMKATYIN LKPARKYRFH.

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    Cuedc2 Human
  • View Data Sheet

    Name :

    DNALI1 Human

    Description:

    Dynein Axonemal Light Intermediate Chain 1 Human Recombinant

    Dynein, Axonemal, Light Intermediate Chain 1, DJ423B22.5 (Axonemal Dynein Light Chain (Hp28)), Inner Dynein Arm Light Chain Axonemal, hp28, P28, Homolog Of Clamydomonas, Axonemal Dynein Light Intermediate Polypeptide 1, dJ423B22.5, Inner Dynein Arm, Homolog Of Clamydomonas, Dynein, Axonemal, Light Intermediate Polypeptide 1.

    Product # :

    PRO-1756

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    Description

    DNALI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-280 a.a) and having a molecular mass of 34.2kDa. DNALI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DNALI1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dynein Axonemal Light Intermediate Chain1 also known as DNALI1 belongs to the inner dynein arm light chain family. DNALI1 take a dynamic role in flagellar motility. DNALI1 is the human homolog of the Chlamydomonas inner dynein arm gene, p28. The exactfunction of DNALI1 is not known yet, on the other hand, it is a potential candidate for immotile cilia syndrome. In addition it has been found that the following diseases: primary ciliary dyskinesia, and huntington's disease have been associated with DNALI1. Ultrastructural defects of the inner dynein arms are seen in patients with ICS. Immotile mutant strains ofChlamydomonas, biflagellated algae, show similar defects.

    • Synonyms

      Dynein, Axonemal, Light Intermediate Chain 1, DJ423B22.5 (Axonemal Dynein Light Chain (Hp28)), Inner Dynein Arm Light Chain Axonemal, hp28, P28, Homolog Of Clamydomonas, Axonemal Dynein Light Intermediate Polypeptide 1, dJ423B22.5, Inner Dynein Arm, Homolog Of Clamydomonas, Dynein, Axonemal, Light Intermediate Polypeptide 1.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMVTANKA HTGQGSCWVA TLASAMIPPA DSLLKYDTPV LVSRNTEKRS PKARLLKVSP QQPGPSGSAP QPPKTKLPST PCVPDPTKQA EEILNAILPP REWVEDTQLW IQQVSSTPST RMDVVHLQEQ LDLKLQQRQA RETGICPVRR ELYSQCFDEL IREVTINCAE RGLLLLRVRD EIRMTIAAYQ TLYESSVAFG MRKALQAEQG KSDMERKIAE LETEKRDLER QVNEQKAKCE ATEKRESERR QVEEKKHNEE IQFLKRTNQQ LKAQLEGIIA PKK

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    Dnali1 Human
  • View Data Sheet

    Name :

    CCL6 Mouse

    Description:

    C-10 Mouse Recombinant (CCL6)

    Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.

    Product # :

    CHM-307

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    Description

    C-10 Mouse Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.7kDa.The CCL6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCL6 Mouse was 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 was determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25µg/ml.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 6 (CCL6) is a small cytokine belonging to the CC chemokine family that has only been identified in rodents.
      In mice, CCL6 is expressed in cells from neutrophil and macrophage lineages, and can be greatly induced under conditions suitable for myeloid cell differentiation. It is highly expressed in bone marrow cultures that have been stimulated with the cytokine GM-CSF. Some low levels of gene expression also occur in certain cell lines of myeloid origin (e.g. the immature myeloid cell lines DA3 and 32D cl3, and the macrophage cell line P388D) that can also be greatly induced in culture with GM-CSF. However, in activated T cell lines, expression of CCL6 is greatly reduced. CCL6 can also be induced in the mouse lung by the cytokine interleukin 13. Mouse CCL6 is located on chromosome 11. The cell surface receptor for CCL6 is believed to be the chemokine receptor CCR1.

    • Synonyms

      Small inducible cytokine A6, CCL6, C10 protein, c10, MRP-1, Scya6, chemokine (C-C motif) ligand 6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized C10 protein although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL6 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 C10 protein in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      GLIQEIEKED RRYNPPIIHQ GFQDTSSDCC FSYATQIPCK RFIYYFPTSG GCIKPGIIFI SRRGTQVCAD PSDRRVQRCL STLKQGPRSG NKVIA.

    • Background

      What is the molecular weight/Mw of CCL6 MOUSE Protein?
      CCL6 MOUSE Protein has a total Mw of 10.7kDa.

      What is the source or expression system of CCL6 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL6 MOUSE Protein?
      CCL6 MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL6 MOUSE Protein?
      The Biological activity was determined by its ability to chemoattract human CCR1 transfected BaF3 mouse proB cells using a concentration range of 0.05-0.25µg/ml.

      What is the amino acid sequence of CCL6 MOUSE Protein?
      GLIQEIEKED RRYNPPIIHQ GFQDTSSDCC FSYATQIPCK RFIYYFPTSG GCIKPGIIFI SRRGTQVCAD PSDRRVQRCL STLKQGPRSG NKVIA.

      What applications can CCL6 MOUSE Protein be used in?
      CCL6 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL6 MOUSE Protein?
      The endotoxin level is minimal, CCL6 MOUSE Protein was purified using conventional chromatography techniques.


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    C 10 Mouse
  • View Data Sheet

    Name :

    TBCEL Human

    Description:

    Tubulin Folding Cofactor E-Like Human Recombinant

    Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

    Product # :

    PRO-030

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    Description

    TBCEL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids and having a molecular mass of 50.6kDa. The TBCEL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TBCEL, is a factor that is in charge of the microtubule cytoskeleton in determining cell behavior. TBCEL plays a role as a regulator of tubulin stability. While widely expressed in testis, TBCEL is also present in several tissues at a much lower level. TBCEL comprises of seven LRR (leucine-rich) repeats, one LRRCT domain and one ubiquitin-like domain. The gene that translates TBCEL consists of 66,704 bases and maps to human chromosome 11q23.3. Chromosome 11 houses over 1,400 genes and consist of nearly 4% of the human genome. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are associated with defects in genes that map to chromosome 11.

    • Synonyms

      Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

    • 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 MGSMDQPSGR SFMQVLCEKY SPENFPYRRG PGMGVHVPAT PQGSPMKDRL NLPSVLVLNS CGITCAGDEK EIAAFCAHVS ELDLSDNKLE DWHEVSKIVS NVPQLEFLNL SSNPLNLSVL ERTCAGSFSG VRKLVLNNSK ASWETVHMIL QELPDLEELF LCLNDYETVS CPSICCHSLK LLHITDNNLQ DWTEIRKLGV MFPSLDTLVL ANNHLNAIEE PDDSLARLFP NLRSISLHKS GLQSWEDIDK LNSFPKLEEV RLLGIPLLQP YTTEERRKLV IARLPSVSKL NGSVVTDGER EDSERFFIRY YVDVPQEEVP FRYHELITKY GKLEPLAEVD LRPQSSAKVE VHFNDQVEEM SIRLDQTVAE LKKQLKTLVQ LPTSNMLLYY FDHEAPFGPE EMKYSSRALH SFGIRDGDKI YVESKTK.

    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.

    Tbcel Human
  • View Data Sheet

    Name :

    CBR1 Human

    Description:

    Carbonyl Reductase-1 Human Recombinant

    CBR, hCBR1, SDR21C1, CBR1, Carbonyl reductase [NADPH] 1, NADPH-dependent carbonyl reductase 1, Prostaglandin-E(2) 9-reductase, Prostaglandin 9-ketoreductase, 15-hydroxyprostaglandin dehydrogenase [NADP+], CRN.

    Product # :

    ENZ-415

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    Description

    Recombinant Human CBR1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 277 amino acids (1-277 a.a) and having a molecular mass of 30 kDa. CBR1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CBR1 protein contains 20mM Tris-HCl buffer pH-8.5, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      CBR1 is one of numerous monomeric, NADPH-dependent oxidoreductases having ubiquistly specificity for carbonyl compounds. CBR1 is broadly distributed in human tissues. CBR1 metabolizes toxic environmental quinones and pharmacological relevant substrates. CBR1 converts prostaglandin E2 to prostaglandin F2-alpha.

    • Synonyms

      CBR, hCBR1, SDR21C1, CBR1, Carbonyl reductase [NADPH] 1, NADPH-dependent carbonyl reductase 1, Prostaglandin-E(2) 9-reductase, Prostaglandin 9-ketoreductase, 15-hydroxyprostaglandin dehydrogenase [NADP+], CRN.

    • 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

      MSSGIHVALV TGGNKGIGLA IVRDLCRLFS GDVVLTARDV TRGQAAVQQL QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLDVLVNN AGIAFKVADP TPFHIQAEVT MKTNFFGTRD VCTELLPLIK PQGRVVNVSS IMSVRALKSC SPELQQKFRS ETITEEELVG LMNKFVEDTK KGVHQKEGWP SSAYGVTKIG VTVLSRIHAR KLSEQRKGDK ILLNACCPGW VRTDMAGPKA TKSPEEGAET PVYLALLPPD AEGPHGQFVS EKRVEQW.

    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.

    Cbr1 Human
  • View Data Sheet

    Name :

    LYN Human

    Description:

    v-yes-1 Yamaguchi Sarcoma Viral Related Oncogene Human Recombinant

    Tyrosine-protein kinase Lyn, Lck/Yes-related novel protein tyrosine kinase, V-yes-1 Yamaguchi sarcoma viral related oncogene homolog, p53Lyn, p56Lyn, JTK8, EC 2.7.10, LYN Proto-Oncogene, Src Family Tyrosine Kinase, V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog, Lck/Yes-Related Novel Protein Tyrosine Kinase, EC 2.7.10.2.

    Product # :

    PRO-136

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    Description

    LYN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 535 amino acids (1-512) and having a molecular mass of 61.0kDa. LYN is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The LYN 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.

    More Info

    • Introduction

      Tyrosine-protein kinase Lyn (LYN) belongs to the src family of non-receptor protein tyrosine kinases, which is primarily expressed in haematopoietic tissues. LYN protein is involved in induction of stress-activated protein kinase (SAPK), but not ERK or p38 MAPK, in response to genotoxic agents. LYN protein stimulates SAPK by a MKK7- and MEKK1-dependent mechanism. The LYN - MEKK1 - MKK7 - SAPK pathway is efficient in the induction of apoptosis by genotoxic agents.

    • Synonyms

      Tyrosine-protein kinase Lyn, Lck/Yes-related novel protein tyrosine kinase, V-yes-1 Yamaguchi sarcoma viral related oncogene homolog, p53Lyn, p56Lyn, JTK8, EC 2.7.10, LYN Proto-Oncogene, Src Family Tyrosine Kinase, V-Yes-1 Yamaguchi Sarcoma Viral Related Oncogene Homolog, Lck/Yes-Related Novel Protein Tyrosine Kinase, EC 2.7.10.2.

    • 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 MGSMGCIKSK GKDSLSDDGV DLKTQPVRNT ERTIYVRDPT SNKQQRPVPE SQLLPGQRFQ TKDPEEQGDI VVALYPYDGI HPDDLSFKKG EKMKVLEEHG EWWKAKSLLT KKEGFIPSNY VAKLNTLETE EWFFKDITRK DAERQLLAPG NSAGAFLIRE SETLKGSFSL SVRDFDPVHG DVIKHYKIRS LDNGGYYISP RITFPCISDM IKHYQKQADG LCRRLEKACI SPKPQKPWDK DAWEIPRESI KLVKRLGAGQ FGEVWMGYYN NSTKVAVKTL KPGTMSVQAF LEEANLMKTL QHDKLVRLYA VVTREEPIYI ITEYMAKGSL LDFLKSDEGG KVLLPKLIDF SAQIAEGMAY IERKNYIHRD LRAANVLVSE SLMCKIADFG LARVIEDNEY TAREGAKFPI KWTAPEAINF GCFTIKSDVW SFGILLYEIV TYGKIPYPGR TNADVMTALS QGYRMPRVEN CPDELYDIMK MCWKEKAEER PTFDYLQSVL DDFYTATEGQ YQQQP.

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    Lyn Human
  • View Data Sheet

    Name :

    CCL7 Mouse

    Description:

    Monocyte Chemotactic Protein-3 Mouse Recombinant (CCL7)

    Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.

    Product # :

    CHM-318

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    Description

    Monocyte Chemotactic Protein-3 Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 74 amino acids and having a molecular mass of 8510 Dalton. The MCP-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined by the ability of Mouse MCP-3 to chemoattract Balb/C mouse spleen MNCs at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 7 (CCL7) is a small cytokine known as a chemokine that was previously called monocyte-specific chemokine 3 (MCP3). Due to CCL7 possessing two adjacent N-terminal cysteine residues in its mature protein, it is classified among the subfamily of chemokines known as CC chemokines. CCL7 specifically attracts monocytes, and regulates macrophage function. It is produced by certain tumor cell lines and by macrophages. This chemokine is located on chromosome 17 in humans, in a large cluster containing many other CC chemokines and is most closely related to CCL2(previously called MCP1).

    • Synonyms

      Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MCP-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL7 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 Monocyte Chemotactic Protein-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QPDGPNASTC CYVKKQKIPK RNLKSYRRIT SSRCPWEAVI FKTKKGMEVC AEAHQKWVEE AIAYLDMKTP TPKP.

    • Background

      What is the molecular weight/Mw of CCL7 MOUSE Protein?
      CCL7 MOUSE Protein has a total Mw of 8.51kDa.

      What is the source or expression system of CCL7 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL7 MOUSE Protein?
      CCL7 MOUSE Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL7 MOUSE Protein?
      The specific activity as determined by the ability of Mouse MCP-3 to chemoattract Balb/C mouse spleen MNCs at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL7 MOUSE Protein?
      QPDGPNASTC CYVKKQKIPK RNLKSYRRIT SSRCPWEAVI FKTKKGMEVC AEAHQKWVEE AIAYLDMKTP TPKP.

      What applications can CCL7 MOUSE Protein be used in?
      CCL7 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL7 MOUSE Protein?
      The endotoxin level is minimal, CCL7 MOUSE 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.

    Mcp 3 Mouse
  • View Data Sheet

    Name :

    RHOG Human

    Description:

    Ras Homolog Gene Family Member G Human Recombinant

    Ras homolog family member G(rho G), rho-related GTP-binding protein RhoG, MGC125836, RhoG, ARHG, MGC125835.

    Product # :

    PRO-1136

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    Description

    RHOG Human Recombinant produced in E. coli is a single polypeptide chain containing 225 amino acids (1-188) and having a molecular mass of 25.2 kDa. RHOG is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RHOG solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.5M NaCl, 50mM Imidazole and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RHOG belongs to the Rac subfamily of the Rho family of small G proteins. RHOG is a small monomeric GTP-binding protein (G protein), and is a key element of several intracellular signalling pathways. RHOG is needed for the formation of membrane ruffles during macropinocytosis. RHOG takes part in cell migration and is essential for the formation of cup-like structures during trans-endothelial migration of leukocytes. Similar to various small G proteins RHOG has a role in several cellular signalling mechanisms such as cell motility, gene transcription, endocytosis, neurite outgrowth, protection from anoikis and regulation of the neutrophil NADPH oxidase.

    • Synonyms

      Ras homolog family member G(rho G), rho-related GTP-binding protein RhoG, MGC125836, RhoG, ARHG, MGC125835.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMQS IKCVVVGDGA VGKTCLLICY TTNAFPKEYI PTVFDNYSAQ SAVDGRTVNL NLWDTAGQEE YDRLRTLSYP QTNVFVICFS IASPPSYENV RHKWHPEVCH HCPDVPILLV GTKKDLRAQP DTLRRLKEQG QAPITPQQGQ ALAKQIHAVR YLECSALQQD GVKEVFAEAV RAVLNPTPIK RGRSC

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    Rhog Human
  • View Data Sheet

    Name :

    FLAG PAT3G6AT antibody

    Description:

    FLAG peptide Clone PAT3G6AT, Mouse Anti Human

    Product # :

    ANT-736

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      A fusion tag called FLAG consists of eight amino acids (AspTyrLysAspAspAspAspLys) including an enterokinase-cleavage site. FLAG is specifically designed for immunoaffinity chromatography. It allows elution under non-denaturing conditions. Several antibodies against this peptide have been developed. One antibody denoted as M1 binds the peptide in the presence of bivalent metal cations preferably Ca(+). Elution is effected by chelating agents. Another strategy is competitive elution with excess of free Flag Peptide. The FLAG peptide purifies and detects recombinant fusion proteins. FLAG peptide is useful in Western blotting, immunocytochemistry, immunoprecipitation, flow cytometry, protein purification, and in the study of protein-protein interactions, cell ultrastructure, and protein localization. Flag peptide is a hydrophilic tag which significantly improves the detection and purification of recombinant fusion proteins.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human FLAG mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a Synthetic peptide (DYKDDDDKC)-KLH.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT3G6AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      FLAG antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Flag Antibody
  • View Data Sheet

    Name :

    CYGB Human

    Description:

    Cytoglobin Human Recombinant

    HGB, STAP, Cytoglobin, CYGB.

    Product # :

    PRO-842

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    Description

    CYGB 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 23.5kDa. The CYGB is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CYGB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytoglobin is a globin protein found in the brain and is mainly utilized in marine mammals. CYGB acts a a protector under conditions of hypoxia. The suggested function of CYGB is the modulation of oxygen and nitric oxide metabolism or scavenging free radicals within a cell.

    • Synonyms

      HGB, STAP, Cytoglobin, CYGB.

    • 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 MEKVPGEMEI ERRERSEELS EAERKAVQAM WARLYASCED VGVAILVRFF VNFPSAKQYF SQFKHMEDPL EMERSPQLRK HACRVMGALN TVVENLHDPD KVSSVLALVG KAHALKHKVE PVYFKILSGV ILEVVAEEFA SDFPPETQRA WAKLRGLIYS HVTAAYKEVG WVQQVPNATT PPATLPSSGP.

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    Cygb Human
  • View Data Sheet

    Name :

    Inhibin a Human

    Description:

    Inhibin Alpha Human Recombinant

    Product # :

    HOR-303

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    Description

    Inhibin-Alpha Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 264 amino acids comprising of both A and B chains, having a molecular mass of 33.5 kDa.The Inhibin-Alpha is fused with an amino-terminal hexahistidine tag. The Inhibin-Alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Inhibin-A alpha chain is supplied in 20mM Tris and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE analysis.

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      Alpha chain:
      STPLMSWPWSPSALRLLQRPPEEPAAHANCHRVALNISFQELGWERWIVYPPSFIFHYCHGGCGLHIP PNLSLPVPGAPPTPAQPYSLLPGAQPCCAALPGTMRPLHVRTTSDGGYSFKYETVPNLLTQHCACI.

      Beta Chain:
      GLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMR
      GHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

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    Inhibin A Human
  • View Data Sheet

    Name :

    CST3 Protein, His

    Description:

    Cystatin-C Human Recombinant, His Tag

    Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    Product # :

    PRO-656

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    Description

    Cystatin-C Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 129 amino acids and having a molecular mass of 14.5 kDa. The protein contains an extra His tag at N-terminus. The Cystatin-C amino acid sequence is identical to UniProtKB/Swiss-Prot entry Q6FGW9 amino acids 28–146.The Cystatin-C is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. 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.

    • Solubility

      Add deionized water to prepare a working stock solution of approximately 0.5mg/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.

    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.

    Cystatin C Human Recombinant
  • View Data Sheet

    Name :

    DKK3 Human, HEK

    Description:

    Dickkopf-Related Protein 3 Human Recombinant, HEK

    Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    Product # :

    PRO-1638

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    Description

    DKK3 Human Recombinant is a single polypeptide chain containing 337 amino acids (22-350). DKK3 is fused to 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    DKK3 was lyophilized from a 0.2µM filtered solution of 20mM PB and 150mM NaCl, pH 7.2.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dickkopf-related protein 3 (DKK3) belongs to the DKK protein family including Dkk-1, 2, 3 and -4. DKK3 is a 350 amino acid secreted glycoprotein which is comprised of an N-terminal signal peptide and 2 conserved cysteine-rich domains that are separated by a 12 amino acid linker region. DKK3 is involved in embryonic development through its inhibition of the WNT signaling pathway. DKK3 gene expression is decreased in a variety of cancer cell lines and it may act as a tumor suppressor gene.

    • Synonyms

      Dickkopf 3 homolog (Xenopus laevis), dickkopf-related protein 3, regulated in glioma, RIG, RIG-like 7-1, RIG-like 5-6, Dkk-3, REIC.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized DKK3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DKK3 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 DKK3 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APAPTATSAPVKPGPALSYPQEEATLNEMFREVEELMEDTQHKLRSAVEEMEAEEAAA
      KASSEVNLANLPPSYHNETNTDTKVGNNTIHVHREIHKITNNQTGQMVFSETVITSVG
      DEEGRRSHECIIDEDCGPSMYCQFASFQYTCQPCRGQRMLCTRDSECCGDQLCVWGHC
      TKMATRGSNGTICDNQRDCQPGLCCAFQRGLLFPVCTPLPVEGELCHDPASRLLDLIT
      WELEPDGALDRCPCASGLLCQPHSHSLVYVCKPTFVGSRDQDGEILLPREVPDEYEVG
      SFMEEVRQELEDLERSLTEEMALGEPAAAAAALLGGEEIVDHHHHHH.

    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.

    Dkk3 Human Hek
  • View Data Sheet

    Name :

    TCEAL1 Human

    Description:

    Transcription Elongation Factor A (SII)-Like 1 Human Recombinant

    Transcription elongation factor A protein-like 1, TCEA-like protein 1, Nuclear phosphoprotein p21/SIIR, Transcription elongation factor S-II protein-like 1, TCEAL1, SIIR, p21, pp21.

    Product # :

    PRO-507

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TCEAL1 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 167 amino acids (1-159 a.a.) and having a molecular mass of 19.7kDa. The TCEAL1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TCEAL1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transcription elongation factor A protein-like 1 (TCEAL1) is a member of the transcription elongation factor A (SII)-like (TCEAL) family, which may function as nuclear phosphoproteins that modulate transcription in a promoter context-dependent manner. TCEAL1 is involved in transcriptional regulation. TCEAL1 is expressed in all tissues, especially highly expressed in the heart, ovary, prostate and skeletal muscle.

    • Synonyms

      Transcription elongation factor A protein-like 1, TCEA-like protein 1, Nuclear phosphoprotein p21/SIIR, Transcription elongation factor S-II protein-like 1, TCEAL1, SIIR, p21, pp21.

    • 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

      MDKPRKENEE EPQSAPKTDE ERPPVEHSPE KQSPEEQSSE EQSSEEEFFP EELLPELLPE MLLSEERPPQ EGLSRKDLFE GRPPMEQPPC GVGKHKLEEG SFKERLARSR PQFRGDIHGR NLSNEEMIQA ADELEEMKRV RNKLMIMHWK AKRSRPYPIL EHHHHHH.

    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.

    Tceal1 Human
  • View Data Sheet

    Name :

    KLK10 Human

    Description:

    Kallikrein-10 Human Recombinant

    Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.

    Product # :

    ENZ-795

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    • description
    • source
    • formulation
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    • More Info

    Description

    KLK10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (34-276) and having a molecular mass of 29.1kDa.KLK10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KLK10 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikrein-10 (KLK10) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. Kallikreins are a subgroup of serine proteases having various physiological functions. KLK10 is secreted and has a role in suppression of tumorigenesis in breast and prostate cancers.

    • Synonyms

      Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.

    • 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 MGSALLPQND TRLDPEAYGS PCARGSQPWQ VSLFNGLSFH CAGVLVDQSW VLTAAHCGNK PLWARVGDDH LLLLQGEQLR RTTRSVVHPK YHQGSGPILP RRTDEHDLML LKLARPVVLG PRVRALQLPY RCAQPGDQCQ VAGWGTTAAR RVKYNKGLTC SSITILSPKE CEVFYPGVVT NNMICAGLDR GQDPCQSDSG GPLVCDETLQ GILSWGVYPC GSAQHPAVYT QICKYMSWIN KVIRSN.

    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.

    Klk10 Human
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