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Search results

1000 results found for “Cofilin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    NEFL Human

    Description:

    Neurofilament Light Human Recombinant

    Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    Product # :

    PRO-2584

    Price :

    Quantity :

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    • description
    • source
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    • purity
    • More Info

    Description

    NEFL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (2-543 a.a) containing 551 amino acids including a 9 a.a N-terminal His tag. The total molecular mass is 62.5kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    NEFL filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in 15mM Tris and 85mM Glycine, pH 8.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NEFL or Neurofilament light polypeptide is a protein that is encoded through the NEFL gene. NEFL is correlated to a disease called Charcot–Marie–Tooth. The protein’s light subunit is determined by immunoassays in the plasma and cerebrospinal fluid, if present, it can indicate on axonal damage in neurological diseases. By doing so, NEFL can act as a marker for Huntington's disease, Amyotrophic Lateral Sclerosis and multiple sclerosis.

    • Synonyms

      Neurofilament light polypeptide, NF-L, NEFL, NF68, NFL, 68 kDa neurofilament protein.

    • 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 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MKHHHHHHAS SFSYEPYYST SYKRRYVETP RVHISSVRSG YSTARSAYSS YSAPVSSSLS VRRSYSSSSG SLMPSLENLD LSQVAAISND LKSIRTQEKA QLQDLNDRFA SFIERVHELE QQNKVLEAEL LVLRQKHSEP SRFRALYEQE IRDLRLAAED ATNEKQALQG EREGLEETLR NLQARYEEEV LSREDAEGRL MEARKGADEA ALARAELEKR IDSLMDEISF LKKVHEEEIA ELQAQIQYAQ ISVEMDVTKP DLSAALKDIR AQYEKLAAKN MQNAEEWFKS RFTVLTESAA KNTDAVRAAK DEVSESRRLL KAKTLEIEAC RGMNEALEKQ LQELEDKQNA DISAMQDTIN KLENELRTTK SEMARYLKEY QDLLNVKMAL DIEIAAYRKL LEGEETRLSF TSVGSITSGY SQSSQVFGRS AYGGLQTSSY LMSTRSFPSY YTSHVQEEQI EVEETIEAAK AEEAKDEPPS EGEAEEEEKD KEEAEEEEAA EEEEAAKEES EEAKEEEEGG EGEEGEETKE AEEEEKKVEG AGEEQAAKKK D.

    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.

    Hepsin Human
  • View Data Sheet

    Name :

    ATF Bovine

    Description:

    Apo Transferrin Bovine

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.

    Product # :

    PRO-511

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • More Info

    Description

    Bovine Apo Transferrin is a glycoprotein of approximately 77kDa.

    Source

    Bovine Serum.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
      Bovine Transferrin is a crucial component for the cultivation of mammalian cells in- vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin are Molecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.

    • Physical Appearance

      Sterile Filtered off-white lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Apo Transferrin between 2-8°C, do not freeze.

    • Solubility

      It is recommended to reconstitute the lyophilized Apo Transferrin in sterile 18MΩ-cm H2O not less than 1gr/30ml in 20min. at 20-25C.

    • Iron Content

      The Iron content was estimated by ICP-OES and was found to be less than 40 ppm.

    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.

    Apo Transferrin Bovine
  • View Data Sheet

    Name :

    EFNA1 Human

    Description:

    Ephrin A1 Human Recombinant

    Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    Product # :

    PRO-971

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • formulation
    • purity
    • More Info

    Description

    EFNA1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (19-182) and having a molecular mass of 21.6 kDa.EFNA1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EFNA1 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.

    More Info

    • Introduction

      EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.

    • Synonyms

      Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    • 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 MDRHTVFWNS SNPKFRNEDY TIHVQLNDYV DIICPHYEDH SVADAAMEQY ILYLVEHEEY QLCQPQSKDQ VRWQCNRPSA KHGPEKLSEK FQRFTPFTLG KEFKEGHSYY YISKPIHQHE DRCLRLKVTV SGKITHSPQA HVNPQEKRLA ADDPEVRVLH SIGHS

    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.

    Efna1 Human
  • View Data Sheet

    Name :

    NXPH1 Human

    Description:

    Neurexophilin 1 Human Recombinant

    Nbla00697, NPH1, Neurexophilin-1, NXPH1.

    Product # :

    PRO-1859

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • formulation
    • purity
    • More Info

    Description

    NXPH1 Human Recombinant produced in E. coli is. a single polypeptide chain containing 273 amino acids (22-271) and having a molecular mass of 31kDa. NXPH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NXPH1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neurexophilin 1 (NXPH1) is a part of the neurexophilin family which encodes a secreted protein with a variable N terminal domain, an extremely conserved, N-glycosylated central domain, a short linker region, and a cysteine-rich Cterminal domain. NXPH1 shapes a very tight complex with alpha neurexins, a group of proteins which promote adhesion among dendrites and axons.

    • Synonyms

      Nbla00697, NPH1, Neurexophilin-1, NXPH1.

    • 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 MGSANLTNGG KSELLKSGSS KSTLKHIWTE SSKDLSISRL LSQTFRGKEN DTDLDLRYDT PEPYSEQDLW DWLRNSTDLQ EPRPRAKRRP IVKTGKFKKM FGWGDFHSNI KTVKLNLLIT GKIVDHGNGT FSVYFRHNST GQGNVSVSLV PPTKIVEFDL AQQTVIDAKD SKSFNCRIEY EKVDKATKNT LCNYDPSKTC YQEQTQSHVS WLCSKPFKVI CIYISFYSTD YKLVQKVCPD YNYHSDTPYF PSG.

    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.

    Nxph1 Human
  • View Data Sheet

    Name :

    CALM2 Human

    Description:

    Calmodulin-2 Human Recombinant

    PHKD, CAMII, PHKD2, Calmodulin-2, CALM2, CALM1 protein, Phosphorylase kinase delta.

    Product # :

    PRO-618

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    Recombinant CALM2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids and having a molecular mass of 16 kDa. CALM2 is purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The CALM2 solution (1mg/ml) contains 20mM Tris-HCl, pH-7.5.

    Purity

    Greater than 90.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Calmodulin-2 acts as an intracellular calcium sensor protein. When the intracellular Ca2+ concentration increases, calmodulin can bind up to four Ca2+, changing its conformation and regulating cellular functions such as activation or inhibition of a large number of enzymes, ion channels, and receptors. P53 protein stimulates CALM2 gene expression in 041 cells. CALM-2 is involved in the processes of Ca(2+)-induced neuronal cell death and the blockage of calmodulin attenuates brain injury after cerebral ischemia. Calmodulin-2 mediates the control of a large number of enzymes and other proteins by ca(2+). among the enzymes to be stimulated by the calmodulin-ca(2+) complex are a number of protein kinases and phosphatases.

    • Synonyms

      PHKD, CAMII, PHKD2, Calmodulin-2, CALM2, CALM1 protein, Phosphorylase kinase delta.

    • 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

      MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK.

    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.

    Calm2 Human
  • View Data Sheet

    Name :

    TFF2 Human

    Description:

    Trefoil Factor-2 Human Recombinant

    TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

    Product # :

    CYT-612

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    Description

    TFF-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 106 amino acids (24-129) and having a total molecular mass of 12 kDa. TFF2 Human Recombinant includes a 40-amino acid trefoil motif containing three conserved intramolecular disulfide bonds and was purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TFF2 protein was lyophilized from 0.4μm filtered solution at a concentration of 1mg/mL containing 1x 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 human MCF-7 cells using a concentration 1.0-10.0 ng/ml.

    More Info

    • Introduction

      Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains.

    • Synonyms

      TFF-2, Spasmolytic polypeptide, Spasmolysin, SML1, Trefoil factor 2, SP, TFF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF2 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 TFF2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EKPSPCQCSR LSPHNRTNCG FPGITSDQCF DNGCCFDSSV TGVPWCFHPL PKQESDQCVM EVSDRRNCGY PGISPEECAS RKCCFSNFIF EVPWCFFPKSVEDCHY.

    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.

    Tff2 Human
  • View Data Sheet

    Name :

    CAPSL Human

    Description:

    Calcyphosine-Like Human Recombinant

    Calcyphosine-like protein, CAPSL, MGC26610.

    Product # :

    PRO-185

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    Description

    CAPSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 228 amino acids (1-208) and having a molecular mass of 26.3 kDa.The CAPSL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CAPSL protein at 1mg/ml in 20mM Tris-HCL, pH-8, 0.2M NaCl, 5mM DTT and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CAPSL is a calcium-binding protein holding two conserved calcium-binding motifs (EF-hands) which are found in a superfamily of calcium sensors and calcium signal modulators. In addition, the CAPSL gene is in the same linkage disequilibrium (LD) block as the IL7R gene and there is well known association between the CAPSL-IL7R locus and type 1 diabetes.

    • Synonyms

      Calcyphosine-like protein, CAPSL, MGC26610.

    • Physical Appearance

      CAPSL is supplied as a 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 MAGTARHDRE MAIQAKKKLT TATDPIERLR LQCLARGSAG IKGLGRVFRI MDDDNNRTLD FKEFMKGLND YAVVMEKEEV EELFQRFDKD GNGTIDFNEF LLTLRPPMSR ARKEVIMQAF RKLDKTGDGV ITIEDLREVY NAKHHPKYQN GEWSEEQVFR KFLDNFDSPY DKDGLVTPEE FMNYYAGVSA SIDTDVYFII MMRTAWKL

    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.

    Capsl Human
  • View Data Sheet

    Name :

    CCL28 Human

    Description:

    Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28)

    MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    Product # :

    CHM-353

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    Description

    CCL28 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 108 amino acids and having a molecular mass of 12.3 kDa. The CCL28 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM PBS and 150mM 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 lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
      Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

    • Synonyms

      MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL28 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL28 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 CCL28 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.

    • Background

      What is the molecular weight/Mw of CCL28 HUMAN Protein?
      CCL28 HUMAN Protein has a total Mw of 12.3kDa.

      What is the source or expression system of CCL28 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL28 HUMAN Protein?
      CCL28 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL28 HUMAN Protein?
      Determined by its ability to chemoattract human lymphocytes using a concentration range of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CCL28 HUMAN Protein?
      SEAILPIASS CCTEVSHHIS RRLLERVNMC RIQRADGDCD LAAVILHVKR RRICVSPHNH TVKQWMKVQA AKKNGKGNVC HRKKHHGKRN SNRAHQGKHE TYGHKTPY.

      What applications can CCL28 HUMAN Protein be used in?
      CCL28 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL28 HUMAN Protein?
      The endotoxin level is minimal, CCL28 HUMAN Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ccl28 Human
  • View Data Sheet

    Name :

    PF4V1 Human

    Description:

    Platelet Factor 4 Variant 1 Human Recombinant

    PF4V1, Platelet Factor 4 Variant 1, CXCL4L1, CXCL4V1, PF4alt, PF4var1, SCYB4V1, PF4-ALT, PF4A, C-X-C Motif Chemokine 4, Platelet Factor 4 Variant, Platelet Factor 4, Variant 1 (PF4-Like) , C-X-C Motif Chemokine 4 Variant.

    Product # :

    CHM-027

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    Description

    PF4V1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids (31-104 a.a.) and having a molecular mass of 10.6kDa.PF4V1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PF4V1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Platelet Factor 4 Variant 1 (PF4V1) is a member of the intercrine alpha (chemokine CxC) family. PF4V1 is an inhibitor of angiogenesis and inhibitor of endothelial cell chemotaxis (in vitro).

    • Synonyms

      PF4V1, Platelet Factor 4 Variant 1, CXCL4L1, CXCL4V1, PF4alt, PF4var1, SCYB4V1, PF4-ALT, PF4A, C-X-C Motif Chemokine 4, Platelet Factor 4 Variant, Platelet Factor 4, Variant 1 (PF4-Like) , C-X-C Motif Chemokine 4 Variant.

    • Physical Appearance

      Sterile Filtered colorless 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 MGSFARAEAE EDGDLQCLCV KTTSQVRPRH ITSLEVIKAG PHCPTAQLIA TLKNGRKICL DLQALLYKKI IKEHLES.

    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.

    Pf4V1 Human
  • View Data Sheet

    Name :

    CHGB Human

    Description:

    Chromogranin B Human Recombinant

    SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.

    Product # :

    PRO-824

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    Description

    CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    The CHGB protein 0.25mg/ml solution containing 20mM Tris-HCl pH-8, 0.15M NaCl & 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      CHGB is a neuroendocrine secretory granule protein, that is the precursor for other biologically active peptides. CHGB is part of the chromogranin/secretogranin protein family and is expressed in the adrenal medulla, and in pheochromocytoma.

    • Synonyms

      SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.

    • 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 MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EEAGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA AMDLELQKIA EKFSQRG.

    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.

    Chgb Human
  • View Data Sheet

    Name :

    CTACK Human

    Description:

    CTACK Human Recombinant (CCL27)

    ALP, CTACK, ESKINE, ILC, PESKY, SCYA27, CCL27, C-C motif chemokine 27, Small-inducible cytokine A27, IL-11 R-alpha-locus chemokine, Skinkine, ESkine, Cutaneous T-cell-attracting chemokine.

    Product # :

    CHM-373

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    • SDS-PAGE

    Description

    CTACK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 89 amino acids (25-112 a.a.) and having a molecular mass of 10.3kDa. CTACK protein is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CTACK Human solution containing 10mM sodium citrate pH-3.5 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    SDS-PAGE

    CTACK Human-SDS-PAGE - Product image 1

    More Info

    • Introduction

      CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.

    • Synonyms

      ALP, CTACK, ESKINE, ILC, PESKY, SCYA27, CCL27, C-C motif chemokine 27, Small-inducible cytokine A27, IL-11 R-alpha-locus chemokine, Skinkine, ESkine, Cutaneous T-cell-attracting chemokine.

    • 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

      MFLLPPSTAC CTQLYRKPLS DKLLRKVIQV ELQEADGDCH LQAFVLHLAQ RSICIHPQNP SLSQWFEHQE RKLHGTLPKL NFGMLRKMG.

    • Background

      What is the molecular weight/Mw of CTACK HUMAN Protein?
      CTACK HUMAN Protein has a total Mw of 10.3kDa.

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

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

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

      What is the amino acid sequence of CTACK HUMAN Protein?
      MFLLPPSTAC CTQLYRKPLS DKLLRKVIQV ELQEADGDCH LQAFVLHLAQ RSICIHPQNP SLSQWFEHQE RKLHGTLPKL NFGMLRKMG.

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

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

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ctack Human
  • View Data Sheet

    Name :

    HIF1A Human

    Description:

    Hypoxia-Inducible Factor-1 Alpha Human Recombinant

    Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.

    Product # :

    PRO-477

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    Description

    HIF1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (530-826) and having a molecular mass of 32.8kDa. The protein migrates as a 32.8kDa band on SDS-PAGE. The HIF1-A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HIF1A recombinant Human solution (1mg/ml) is formulated in PBS pH-7.4 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hypoxia-inducible factor-1 (HIF-1), identified as one of the transcription factors, has been found to play an essential role in cellular and systemic oxygen homeostasis. HIF-1 is a heterodimer composed of HIF-1b subunit and one of three subunits (Hif-1a, Hif-2 (or Hif-3)). The activation of Hif-1 (is closely associated with a variety of tumors and oncogenic pathways. Hif-1 (consists of DNA binding domain (DBD domain), Dimerization domain and C-terminal regulatory domains, including two transactivation domains (TAD), an oxygen-dependent degradation (ODD) domain, and inhibitory domains. Under hypoxic conditions HIF1A activates the transcription of more than 40 genes, including, erythropoietin, glucose transporters, glycolytic enzymes, VEGF, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. HIF-1A also plays a crucial role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. It binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation involves recruitment of transcriptional coactivators such as CREBPB and EP300. Its activity is improved by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX appears to activate CTAD and potentiates activation by NCOA1 and CREBBP. The induction is under reduced oxygen tension. HIF1A is also induced by a variety of receptor-mediated factors such as growth factors, cytokines, and circulatory factors for example PDGF, EGF, FGF-2, IGF-2, TGF-1 beta, HGF, TNF alpha, IL-1 beta, angiotensin-2 and thrombin. Nevertheless, this induction is less intense than that stimulated by hypoxia.

    • Synonyms

      Hypoxia-inducible factor 1 alpha, HIF-1 alpha, HIF1 alpha, ARNT-interacting protein, Member of PAS protein 1, Basic-helix-loop-helix-PAS protein MOP1, HIF1A, MOP1, HIF1, PASD8, HIF-1A.

    • 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

      MEFKLELVEK LFAEDTEAKN PFSTQDTDLD LEMLAPYIPM DDDFQLRSFD QLSPLESSSA SPESASPQST VTVFQQTQIQ EPTANATTTT ATTDELKTVT KDRMEDIKIL IASPSPTHIH KETTSATSSP YRDTQSRTAS PNRAGKGVIE QTEKSHPRSP NVLSVALSQR TTVPEEELNP KILALQNAQR KRKMEHDGSL FQAVGIGTLL QQPDDHAATT SLSWKRVKGC KSSEQNGMEQ KTIILIPSDL ACRLLGQSMD ESGLPQLTSY DCEVNAPIQG SRNLLQGEEL LRALDQVN.

    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.

    Hif1A Human
  • View Data Sheet

    Name :

    TAC1 Human

    Description:

    Tachykinin-1 Human Recombinant

    Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 1.

    Product # :

    PRO-1338

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    Description

    TAC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 135 amino acids (20-129 a.a) and having a molecular mass of 15.6kDa.TAC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TAC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 2M Urea.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tachykinin-1 (TAC1) belongs to the tachykinin peptide hormone family. TAC1 are a family of peptides which have similar biologic activities and share a common C-terminal sequence, phe-X-gly-leu-met-NH2, however they have distinct N-terminal sequences that convey receptor specificities. TAC1 is assumed to act as neurotransmitters which interact with nerve receptors and smooth muscle cells. TAC1 induces behavioral responses and serves as vasodilators and secretagogues.

    • Synonyms

      Protachykinin-1, Protachykinin 1, 4930528L02Rik, NK-1, NK1, Nka, Nkna, Neurokinin 2, Neurokinin A, Neurokinin alpha, Neuromedin L, Neuropeptide K, Substance P, Tachykinin precursor 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

      MGSSHHHHHH SSGLVPRGSH MGSHMEEIGA NDDLNYWSDW YDSDQIKEEL PEPFEHLLQR IARRPKPQQF FGLMGKRDAD SSIEKQVALL KALYGHGQIS HKRHKTDSFV GLMGKRALNS VAYERSAMQN YERRR.

    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.

    Tac1 Human
  • View Data Sheet

    Name :

    HTF Human

    Description:

    Holo Transferrin Human

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    Product # :

    PRO-315

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    • More Info

    Description

    Human Holo Transferrin is a glycoprotein of approximately 77 kDa.

    Source

    Human serum.

    Formulation

    The protein (10mg/ml) was lyophilized from 20mM NH4HC03 solution.
    May contain traces of buffer salts.

    Purity

    Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
      Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.

    • Physical Appearance

      Sterile Filtered Pink lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Holo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Holo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, HBc, HBV, HAV, HIV and Syphilis.

    • Iron Content

      The Iron content was estimated by ICP and was found to be 1232 ppm.

    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.

    Holo Transferrin Human
  • View Data Sheet

    Name :

    Platelet Factor 4 Bovine

    Description:

    Platelet Factor-4 (CXCL4) Bovine Recombinant

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

    Product # :

    CHM-039

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    Description

    Platelet Factor-4 (CXCL4) Bovine Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 88 amino acid and having a molecular mass of approximately 9.5kDa.PF4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20 mM PB and 500mM NaCl, pH 7.0.

    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 neutrophils is 10-100ng/ml.

    More Info

    • Introduction

      Platelet factor-4 is a 70-amino acid protein that is released from the alpha-granules of activated platelets.PF4’s major physiologic role appears to be neutralization of molecules on the endothelial surface of blood vessels, thereby inhibiting local antithrombin III 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 chemokine family. Furthermore, it is used as an inhibitor in the angiogenesis during tumor therapy.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Platelet Factor-4 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 Platelet Factor-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ESSFPATFVP LPADSEGGED EDLQCVCLKT TSGINPRHIS SLEVIGAGTH CPSPQLLATK KTGRKICLDQ QRPLYKKILK KLLDGDES.

    • Background

      What is the molecular weight/Mw of PLATELET FACTOR 4 BOVINE Protein?
      PLATELET FACTOR 4 BOVINE Protein has a total Mw of 9.5kDa.

      What is the source or expression system of PLATELET FACTOR 4 BOVINE Protein?
      Escherichia Coli.

      What is the Purity of PLATELET FACTOR 4 BOVINE Protein?
      PLATELET FACTOR 4 BOVINE Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of PLATELET FACTOR 4 BOVINE Protein?
      The biological activity determined by a chemotaxis bioassay using human neutrophils is 10-100ng/ml.

      What is the amino acid sequence of PLATELET FACTOR 4 BOVINE Protein?
      ESSFPATFVP LPADSEGGED EDLQCVCLKT TSGINPRHIS SLEVIGAGTH CPSPQLLATK KTGRKICLDQ QRPLYKKILK KLLDGDES.

      What applications can PLATELET FACTOR 4 BOVINE Protein be used in?
      PLATELET FACTOR 4 BOVINE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for PLATELET FACTOR 4 BOVINE Protein?
      The endotoxin level is minimal, PLATELET FACTOR 4 BOVINE 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.

    Cxcl4 Bovine
  • View Data Sheet

    Name :

    WIF1 Human

    Description:

    WNT Inhibitory Factor 1 Human Recombinant

    WIF1, WIF-1, Wnt inhibitory factor 1.

    Product # :

    PRO-684

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    Description

    WIF1 Human is a single, glycosylated polypeptide chain containing 360 amino acids (29-379 a.a.) and having a molecular mass of 39.5 kDaWIF1 is fused to 6 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The WIF1 protein solution contains 1X PBS pH 7.4, 20% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WIF1 binds to wnt proteins and inhibits their activities. WIF1 plays a role in mesoderm segmentation. WNT proteins are extracellular signaling molecules that take part in the control of embryonic development & cancer. WIF1 protein contains a WNT inhibitory factor (WIF) domain and 5 epidermal growth factor (EGF)-like domains. WIF1 takes part in mesoderm segmentation. WIF1 protein is found to be present in fish, amphibia and mammals. WIF1 is a recurrent target in human salivary gland oncogenesis. Downregulation of WIF1 takes part in the development and progression of pleomorphic adenomas. WIF1 is a tumor suppressor, specifically in nonfunctioning pituitary tumors.

    • Synonyms

      WIF1, WIF-1, Wnt inhibitory factor 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

      ADLGPPQEES LYLWIDAHQA RVLIGFEEDI LIVSEGKMAP FTHDFRKAQQ RMPAIPVNIH SMNFTWQAAG QAEYFYEFLS LRSLDKGIMA DPTVNVPLLG TVPHKASVVQ VGFPCLGKQD GVAAFEVDVI VMNSEGNTIL QTPQNAIFFK TCQQAECPGG CRNGGFCNER RICECPDGFH GPHCEKALCT PRCMNGGLCV TPGFCICPPG FYGVNCDKAN CSTTCFNGGT CFYPGKCICP PGLEGEQCEI SKCPQPCRNG GKCIGKSKCK CSKGYQGDLC SKPVCEPGCG AHGTCHEPNK CQCQEGWHGR HCNKRYEASL IHALRPAGAQ LRQHTPSLKK AEERRDPPES NYIWHHHHHH

    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.

    Wif1 Human
  • View Data Sheet

    Name :

    ACTN1 Human

    Description:

    Actinin Alpha 1 Human Recombinant

    ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-1.

    Product # :

    PRO-2227

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    Description

    ACTN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-249 a.a) and having a molecular mass of 31.4kDa. ACTN1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACTN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ACTN1 encodes a nonmuscle, cytoskeletal, alpha actinin isoform and maps to the same site as the structurally similar erythroid beta spectrin gene. Alpha actinins belong to the spectrin gene superfamily which represents a diverse group of cytoskeletal proteins, including the alpha and beta spectrins and dystrophins. Alpha actinin is an actin-binding protein with multiple roles in different cell types. In nonmuscle cells, the cytoskeletal isoform is found along microfilament bundles and adherens-type junctions, where it is involved in binding actin to the membrane. In contrast, skeletal, cardiac, and smooth muscle isoforms are localized to the Z-disc and analogous dense bodies, where they help anchor the myofibrillar actin filaments.

    • Synonyms

      ACTN1, Actinin, Alpha 1, Alpha-Actinin Cytoskeletal Isoform, F-Actin Cross-Linking Protein, Non-Muscle Alpha-Actinin-1, BDPLT15, Actinin 1 Smooth Muscle, Alpha-Actinin-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

      MGSSHHHHHH SSGLVPRGSH MGSEFMDHYD SQQTNDYMQP EEDWDRDLLL DPAWEKQQRK TFTAWCNSHL RKAGTQIENI EEDFRDGLKL MLLLEVISGE RLAKPERGKM RVHKISNVNK ALDFIASKGV KLVSIGAEEI VDGNVKMTLG MIWTIILRFA IQDISVEETS AKEGLLLWCQ RKTAPYKNVN IQNFHISWKD GLGFCALIHR HRPELIDYGK LRKDDPLTNL NTAFDVAEKY LDIPKMLDAE DIVGTARPDE KAIMTYVSSF YHAF.

    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.

    Actn1 Human
  • View Data Sheet

    Name :

    VEGF (121 a.a.) Human

    Description:

    Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-343

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    Description

    Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    VEGF-121 has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 1-6ng/ml corresponding to a specific activity of 166,667-1,000,000U/mg.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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 Vascular Endothelial Growth Factor -121 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENCDKPR R

    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.

    Vegf121 Human
  • View Data Sheet

    Name :

    G CSF Human, PEG

    Description:

    Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

    CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    Product # :

    CYT-018

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    Description

    Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

    Purity

    Greater than 95.0% as determined by SEC-HPLC.

    Biological Activity

    The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

    • Synonyms

      CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    • Physical Appearance

      Colorless, clear and transparent solution.

    • Stability

      G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.

    • Background

      What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

      What is the source or expression system of G CSF HUMAN, PEG Protein?
      Escherichia Coli.

      What is the Purity of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of G CSF HUMAN, PEG Protein?
      The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

      What is the amino acid sequence of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

      What is the endotoxin level for G CSF HUMAN, PEG Protein?
      The endotoxin level is minimal, G CSF HUMAN, PEG 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.

    G Csf Human Pegylated
  • View Data Sheet

    Name :

    Adipsin Human

    Description:

    Complement Factor D Human Recombinant

    Complement factor D, EC 3.4.21.46, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD, ADN.

    Product # :

    PRO-1360

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    Description

    Adipsin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 249 amino acids (26-253 a.a) and having a molecular mass of 26.6kDa.Adipsin is fused to a 21 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor D (Adipsin), which belongs to the trypsin family of peptidases, is involved in the alternative complement pathway of the complement system where it cleaves factor B. In the alternative complement pathway, Adipsin is best known for its role in humoral suppression of infectious agents. In addition, Adipsin is a serine protease which is secreted by adipocytes into the bloodstream. Ultimately, Adipsin has a high level of expression in fat, proposing a role for adipose tissue in immune system biology.

    • Synonyms

      Complement factor D, EC 3.4.21.46, Adipsin, C3 convertase activator, Properdin factor D, CFD, DF, PFD, ADN.

    • 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 MILGGREAEA HARPYMASVQ LNGAHLCGGV LVAEQWVLSA AHCLEDAADG KVQVLLGAHS LSQPEPSKRL YDVLRAVPHP DSQPDTIDHD LLLLQLSEKA TLGPAVRPLP WQRVDRDVAP GTLCDVAGWG IVNHAGRRPD SLQHVLLPVL DRATCNRRTH HDGAITERLM CAESNRRDSC KGDSGGPLVC GGVLEGVVTS GSRVCGNRKK PGIYTRVASY AAWIDSVLA.

    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.

    Adipsin Human
  • View Data Sheet

    Name :

    Eotaxin Human, His

    Description:

    Eotaxin Human Recombinant (CCL11), His Tag

    Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    Product # :

    CHM-344

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    Description

    Eotaxin His Tag Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids fragment (24-87) corresponding to the mature Eotaxin protein and having a molecular mass of 8345.9 Dalton with an amino-terminal hexahistidine tag.The Eotaxin-His is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Eotaxin-His is supplied liquid In Phosphate Buffered Saline pH7.4 containing 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11, MGC22554.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP

    • Background

      What is the molecular weight/Mw of EOTAXIN HUMAN, HIS Protein?
      EOTAXIN HUMAN, HIS Protein has a total Mw of 8.34kDa.

      What is the source or expression system of EOTAXIN HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of EOTAXIN HUMAN, HIS Protein?
      EOTAXIN HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of EOTAXIN HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGPASVPTTC CFNLANRKIP LQRLESYRRI TSGKCPQKAV IFKTKLAKDI CADPKKKWVQ DSMKYLDQKS PTPKP

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

      What is the endotoxin level for EOTAXIN HUMAN, HIS Protein?
      The endotoxin level is minimal, EOTAXIN HUMAN, HIS 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.

    Eotaxin Human His
  • View Data Sheet

    Name :

    PFN1 Rat

    Description:

    Profilin-1 Rat Recombinant

    Profilin-1, Profilin I.

    Product # :

    PRO-2231

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    Description

    PFN1 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-140 a.a) and having a molecular mass of 17.5kDa. PFN1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PFN1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Profilin-1 also known as Pfn1 is a ubiquitous actin monomer-binding protein which is a member of the profilin family. Pfn1 significantly enhances skin wound healing in-vitro as well as in-vivo which is mediated by purinergic receptors. Furthermore, Pfn1 is also active in endothelial cell migration and vessel sprouting. Pfn1 is considered to regulate actin polymerization in response to extracellular signals.

    • Synonyms

      Profilin-1, Profilin I.

    • 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 MGSHMAGWNA YIDSLMADGT CQDAAIVGYK DSPSVWAAVP GKTFVSITPA EVGVLVGKDR SSFFVNGLTL GGQKCSVIRD SLLQDGEFTM DLRTKSTGGA PTFNVTVTMT AKTLVLLMGK EGVHGGLINK KCYEMASHLR RSQY.

    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.

    Pfn1 Rat
  • View Data Sheet

    Name :

    CXCL2 Rat

    Description:

    GRO-beta/MIP-2 Rat Recombinant (CXCL2)

    Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta, CINC-3.

    Product # :

    CHM-372

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    Description

    GRO-Beta Rat Recombinant also called Rat MIP-2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7923 Dalton. The GRO-b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 99.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.

    • Synonyms

      Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta, CINC-3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GRO-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 GRO-beta Rat in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VVVASELRCQ CLTTLPRVDF KNIQSLTVTP PGPHCAQTEV IATLKDGHEV CLNPEAPLVQ RIVQKILNKG KAN.

    • Background

      What is the molecular weight/Mw of CXCL2 RAT Protein?
      CXCL2 RAT Protein has a total Mw of 7.92kDa.

      What is the source or expression system of CXCL2 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL2 RAT Protein?
      CXCL2 RAT Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL2 RAT Protein?
      The biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.

      What is the amino acid sequence of CXCL2 RAT Protein?
      VVVASELRCQ CLTTLPRVDF KNIQSLTVTP PGPHCAQTEV IATLKDGHEV CLNPEAPLVQ RIVQKILNKG KAN.

      What applications can CXCL2 RAT Protein be used in?
      CXCL2 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL2 RAT Protein?
      The endotoxin level is minimal, CXCL2 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.

    Gro B Rat
  • View Data Sheet

    Name :

    Polcalcin Phl p 7

    Description:

    Pollen Allergen Phl p 7 Recombinant

    Polcalcin Phl p 7, Calcium-binding pollen allergen Phl p 7, P7, Phl p 7.

    Product # :

    ALR-015

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Recombinant Polcalcin Phl p 7 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 9.0 kDa. Polcalcin Phl p 7 is purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Polcalcin Phl p 7 is supplied in 20mM HEPES buffer pH-8.0, 0.2M NaCl, 1mM CaCl2 and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phl p 7.0101 is a secondary allergen of timothy grass pollen, which is non-glycosylated protein. Grass pollen-sensitized individuals show IgE antibodies in their blood system. Phl p 7.0101 is a calcium binding protein with similar sequence to pollen antigens that exist in different plants, hence, cross-reactions are possible.

    • Synonyms

      Polcalcin Phl p 7, Calcium-binding pollen allergen Phl p 7, P7, Phl p 7.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Polcalcin Phl P 7
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