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  • Aprotinin

    Aprotinin

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Search results

1000 results found for “Aprotinin”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    Thymosin α1

    Description:

    Thymosin a1 Acetate

    Product # :

    HOR-243

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • formulation
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    • More Info

    Description

    Thymosin a1 acetate, also known as thymalfasin has immunoregulatory properties enhancing immune functions. Thymosin a1 has a molecular formula of C129H215N33O55 a.a. sequence of Ac-Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn-OH and having a Mw of 3108.32 Dalton.

    Formulation

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

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Thymalfasin is a synthetic analogue of thymosin-alpha-1, a 28-amino acid protein derived from the precursor protein prothymosin-alpha. Exhibiting a variety of immunoregulating properties, thymosin-alpha-1 induces differentiation of murine T-cell precursors and human thymocytes and the terminal differentiation of functionally immature cord blood lymphocytes and induces production of IL-2, high affinity IL-2 receptors, and B-cell growth factors by peripheral blood mononuclear cells. T-helper and cytotoxic/suppressor T-cell populations are targets of thymosin activity. Thymosin-alpha-1 has been shown to increase the efficiency of antigen presentation by macrophages and to be an endogenous modulator of alpha-thrombin activity.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymosin a1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymalfasin 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 Thymosin a1 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Thymosin Alpha 1
  • View Data Sheet

    Name :

    RTN4R Human

    Description:

    Reticulon 4 Receptor Human Recombinant

    Reticulon 4 Receptor, Nogo-66 Receptor, Nogo Receptor, NOGOR, NGR , Reticulon-4 Receptor, UNQ330/PRO526.

    Product # :

    PRO-2353

    Price :

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    Description

    RTN4R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 429 amino acids (27-447 a.a.) and having a molecular mass of 46.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57 kDa). RTN4R is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    RTN4R protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Reticulon 4 Receptor, also known as RTN4R, plays a role as a receptor for RTN4, OMG and MAG. RTN4R is a glycosylphosphoinositol (GPI)-anchored protein which is a part from the Nogo recptor family. RTN4R is expressed mainly in neurons and their axons and is regulates axonal regeneration and plasticity in the adult central nervous system. RTN4R is a potential drug target for treating various neurological cases such as spinal cord injury, CNS lesions, stroke and Alzheimer's disease.

    • Synonyms

      Reticulon 4 Receptor, Nogo-66 Receptor, Nogo Receptor, NOGOR, NGR , Reticulon-4 Receptor, UNQ330/PRO526.

    • 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

      CPGACVCYNE PKVTTSCPQQ GLQAVPVGIP AASQRIFLHG NRISHVPAAS FRACRNLTIL WLHSNVLARI DAAAFTGLAL LEQLDLSDNA QLRSVDPATF HGLGRLHTLH LDRCGLQELG PGLFRGLAAL QYLYLQDNAL QALPDDTFRD LGNLTHLFLH GNRISSVPER AFRGLHSLDR LLLHQNRVAH VHPHAFRDLG RLMTLYLFAN NLSALPTEAL APLRALQYLR LNDNPWVCDC RARPLWAWLQ KFRGSSSEVP CSLPQRLAGR DLKRLAANDL QGCAVATGPY HPIWTGRATD EEPLGLPKCC QPDAADKASV LEPGRPASAG NALKGRVPPG DSPPGNGSGP RHINDSPFGT LPGSAEPPLT AVRPEGSEPP GFPTSGPRRR PGCSRKNRTR SHCRLGQAGS GGGGTGDSEG SLEHHHHHH.

    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.

    Rtn4R Human
  • View Data Sheet

    Name :

    S100A11 Human

    Description:

    S100 Calcium Binding Protein A11 Human Recombinant

    Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.

    Product # :

    PRO-385

    Price :

    Quantity :

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    Description

    S100A11 Human Recombinant is expressed in E. coli having a molecular weight of 17kDa fused to an amino terminal hexahistidine tag.

    Source

    Escherichia Coli.

    Formulation

    S100A11 is supplied in PBS and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.
    2 bands on Western blot at 17 and 34 kDa, respectively representing monomeric and dimeric form.

    More Info

    • Introduction

      S100A11 is a member of the S100 family of proteins which contains two EF-hand calcium-binding motifs and is thought to be involved in the regulation of a number of cellular processes including cell cycle progression and differentiation. S100A11 may function in motility, invasion and tubulin polymerisation. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. Chromosomal rearrangements and altered expression of S100A11 have been implicated in tumor metastasis.

    • Synonyms

      Protein S100-A11, S100 calcium-binding protein A11, Calgizzarin, MLN 70, S100A11, MLN70, S100C.

    • Stability

      Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    • Applications

      S100A11 can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
      The biological activity of this product has not yet been tested.

    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.

    S100A11 Human
  • View Data Sheet

    Name :

    CSRP2 Human

    Description:

    Cysteine and Glycine-rich Protein 2 Human Recombinant

    Cysteine and glycine-rich protein 2, Smooth muscle cell LIM protein, LIM domain only 5 smooth muscle, SmLIM, LMO5, CRP2.

    Product # :

    PRO-1096

    Price :

    Quantity :

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    • More Info

    Description

    CSRP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 217 amino acids (1-193) and having a molecular mass of 23.5kDa.CSRP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CSRP2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CSRP2 belongs to the CSRP family. CSRP2 holds 2 LIM zinc-binding domains that take part in regulatory processes essential for development and cellular differentiation. Additionally, CSRP2 is involved in the development of the embryonic vascular system.

    • Synonyms

      Cysteine and glycine-rich protein 2, Smooth muscle cell LIM protein, LIM domain only 5 smooth muscle, SmLIM, LMO5, CRP2.

    • 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 MGSHMPVWGG GNKCGACGRT VYHAEEVQCD GRSFHRCCFL CMVCRKNLDS TTVAIHDEEI YCKSCYGKKY GPKGYGYGQG AGTLNMDRGE RLGIKPESVQ PHRPTTNPNT SKFAQKYGGA EKCSRCGDSV YAAEKIIGAG KPWHKNCFRC AKCGKSLEST TLTEKEGEIY CKGCYAKNFG PKGFGYGQGA GALVHAQ

    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.

    Csrp2 Human
  • View Data Sheet

    Name :

    CSTA Human, Active

    Description:

    Cystatin-A Human Recombinant, Active

    Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.

    Product # :

    PRO-086

    Price :

    Quantity :

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    Description

    Cystatin A Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 118 amino acids (1-98a.a.) and having a molecular mass of 13.1 kDa.The Cystatin A is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cystatin-A (1mg/ml) in 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by reducing SDS-PAGE.

    Biological Activity

    The IC50 value is < 1.0nM. The inhibitory function of CSTA on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25C.

    More Info

    • Introduction

      Human Cystatin A (CSTA or Stefin A) belongs to family 1 of the cystatin superfamily, which is characterized by the lack of disulphide bonds and carbohydrates. CSTA is an intracellular inhibitor regulating the activities of cysteine proteases of the papain family such as Cathepsins B, H and L. Cystatin A has also been implicated in several disease states. Because of altered proteolytic state in cancer progression, CSTA may have a role in the proteolitic pathways.

    • Synonyms

      Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.

    • 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 MIPGGLSEAK PATPEIQEIV DKVKPQLEEK TNETYGKLEA VQYKTQVVAG TNYYIKVRAG DNKYMHLKVF KSLPGQNEDL VLTGYQVDKN KDDELTGF.

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    Csta Human
  • View Data Sheet

    Name :

    HERPUD1 Human

    Description:

    HERPUD1 Human Recombinant

    Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.

    Product # :

    PRO-2105

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    Description

    HERPUD1 Human Recombinant produced in E. coli is a single polypeptide chain containing 286 amino acids (1-263) and having a molecular mass of 31.6kDa.HERPUD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HERPUD1 solution (0.5mg/1ml) contains Phosphate buffer saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HERPUD1 is a multi-pass membrane protein which is a part of the endoplasmic reticulum quality control system. HERPUD1 owns 1 N-terminal ubiquitin-like domain and is expressed highly in the brain. HERPUD1 is also known as ER-associated degradation (ERAD) which takes part in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins.

    • Synonyms

      Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein, HERPUD1, Methyl methanesulfonate (MMF)-inducible fragment protein 1, HERP, KIAA0025, MIF1, Mif1, SUP.

    • 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 MGSMESETEP EPVTLLVKSP NQRHRDLELS GDRGWSVGHL KAHLSRVYPE RPRPEDQRLI YSGKLLLDHQ CLRDLLPKQE KRHVLHLVCN VKSPSKMPEI NAKVAESTEE PAGSNRGQYP EDSSSDGLRQ REVLRNLSSP GWENISRPEA AQQAFQGLGP GFSGYTPYGW LQLSWFQQIY ARQYYMQYLA ATAASGAFVP PPSAQEIPVV SAPAPAPIHN QFPAENQPAN QNAAPQVVVN PGANQNLRMN AQGGPIVEED DEINRD.

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    Herpud1 Human
  • View Data Sheet

    Name :

    DPP4 Human, HEK

    Description:

    Dipeptidyl-Peptidase 4 Human Recombinant, HEK

    CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.

    Product # :

    ENZ-1187

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    Description

    DPP4 Human Recombinant is a single, glycosylated polypeptide chain containing 977 amino acids (29-766a.a) and having a molecular mass of 112.1kDa (calculated). DPP4 is fused to a 239 amino acid hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    DPP4 protein solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

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

    Biological Activity

    Specific activity is > 15,000 pmol/min/ug in which one unit defined as the amount of enzyme that hydrolyze 1pmole of H-Gly-Pro-AMC.HBr to H-Gly-Pro and AMC per minute at pH 8.0 at 37℃.

     The ED50 range ≤250 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike S1 Subunit (CAT# sars-052)..

    The ED50 range ≤200 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike RBD (CAT# sars-054).

    The ED50 range ≤120 ng/ml is measured by its binding ability in a functional ELISA with MERS-CoV Spike (CAT# sars-051).

    More Info

    • Synonyms

      CD26, ADABP, ADCP2, DPPIV, TP103, DPP4, Dipeptidyl peptidase 4, Dipeptidyl peptidase IV, DPP IV, T-cell activation antigen CD26, Adenosine deaminase complexing protein 2, CD26 antigen.

    • 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

      DGSMNKGTDD ATADSRKTYT LTDYLKNTYR LKLYSLRWIS DHEYLYKQEN NILVFNAEYG NSSVFLENST FDEFGHSIND YSISPDGQFI LLEYNYVKQW RHSYTASYDI YDLNKRQLIT EERIPNNTQW VTWSPVGHKL AYVWNNDIYV KIEPNLPSYR ITWTGKEDII YNGITDWVYE EEVFSAYSAL WWSPNGTFLA YAQFNDTEVP LIEYSFYSDE SLQYPKTVRV PYPKAGAVNP TVKFFVVNTD SLSSVTNATS IQITAPASML IGDHYLCDVT WATQERISLQ WLRRIQNYSV MDICDYDESS GRWNCLVARQ HIEMSTTGWV GRFRPSEPHF TLDGNSFYKI ISNEEGYRHI CYFQIDKKDC TFITKGTWEV IGIEALTSDY LYYISNEYKG MPGGRNLYKI QLSDYTKVTC LSCELNPERC QYYSVSFSKE AKYYQLRCSG PGLPLYTLHS SVNDKGLRVL EDNSALDKML QNVQMPSKKL DFIILNETKF WYQMILPPHF DKSKKYPLLL DVYAGPCSQK ADTVFRLNWA TYLASTENII VASFDGRGSG YQGDKIMHAI NRRLGTFEVE DQIEAARQFS KMGFVDNKRI AIWGWSYGGY VTSMVLGSGS GVFKCGIAVA PVSRWEYYDS VYTERYMGLP TPEDNLDHYR NSTVMSRAEN FKQVEYLLIH GTADDNVHFQ QSAQISKALV DVGVDFQAMW YTDEDHGIAS STAHQHIYTH MSHFIKQCFS LPKLLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGK.

    • Background

      DPP4 protein, also known as Dipeptidyl peptidase-4 or CD26, is a cell surface protease with diverse functions in cell signaling and metabolism. This research aims to investigate the role of DPP4 protein in various physiological processes and its implications in disease pathogenesis. Understanding the biological significance of DPP4 can provide insights into its potential as a therapeutic target for several disorders.

      Function of DPP4 Protein:

      DPP4 protein is involved in the cleavage and regulation of several peptide hormones and chemokines, influencing their bioactivity and half-life. It is widely expressed in various tissues, including immune cells, endothelial cells, and epithelial cells. DPP4 can modulate immune responses, glucose metabolism, and neuropeptide signaling through enzymatic and non-enzymatic activities.

      Role of DPP4 Protein in Immune Regulation:

      DPP4 protein plays a role in immune cell activation and regulation. It is expressed on the surface of T cells, where it functions as a co-stimulatory molecule. DPP4 engagement on T cells promotes T cell activation, cytokine production, and adhesion to endothelial cells. Additionally, DPP4 can cleave and inactivate certain chemokines, thereby influencing chemotaxis and immune cell recruitment.

      Implications of DPP4 Protein in Metabolic Disorders:

      DPP4 protein is involved in glucose metabolism and insulin regulation. It cleaves incretin hormones, such as glucagon-like peptide-1 (GLP-1) and gastric inhibitory polypeptide (GIP), which play crucial roles in glucose homeostasis. Inhibition of DPP4 activity can enhance the action of these incretin hormones, leading to improved glycemic control. Therefore, DPP4 inhibitors have been developed as antidiabetic drugs.

      Association of DPP4 Protein with Cardiovascular Diseases:

      DPP4 protein has been implicated in the pathogenesis of cardiovascular diseases. Elevated DPP4 levels have been observed in patients with heart failure, atherosclerosis, and hypertension. DPP4 can contribute to endothelial dysfunction, inflammation, and vascular remodeling, which are key factors in the development and progression of cardiovascular disorders. Inhibition of DPP4 activity has shown potential as a therapeutic strategy in preclinical studies.

      Given its involvement in various biological processes and disease pathogenesis, DPP4 protein has emerged as a potential therapeutic target. DPP4 inhibitors, which prevent the enzymatic activity of DPP4, have been developed for the treatment of type 2 diabetes. These inhibitors enhance the action of incretin hormones, leading to improved glycemic control. Additionally, ongoing research aims to explore the therapeutic potential of DPP4 inhibitors in other conditions, such as immune-mediated disorders and cardiovascular diseases.

      Conclusion:

      The investigation of DPP4 protein provides insights into its diverse functions in cell signaling, immune regulation, and metabolism. Understanding the role of DPP4 in disease pathogenesis opens avenues for the development of targeted therapies for conditions such as diabetes, cardiovascular diseases, and immune-mediated disorders. Further research on DPP4 protein and its associated pathways may uncover new therapeutic opportunities and improve patient outcomes.

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    Dpp4 Human Hek
  • View Data Sheet

    Name :

    IF Human

    Description:

    Intrinsic Factor Human Recombinant

    Gastric intrinsic factor, Intrinsic factor, INF, IF, GIF, IFMH, TCN3, Cobalamin/Vitamin B-12 binding transport protein.

    Product # :

    PRO-375

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    Description

    Intrinsic Factor Human Recombinant produced in baculovirus is a glycosylated, polypeptide chain having a molecular mass of 55,000 Dalton. The Intrinsic Factor is fused to a hexa-histidine at the C-terminus and purified by proprietary chromatographic techniques for removal of bound Vitamin B-12.

    Source

    Sf9 Insect Cells.

    Formulation

    The protein solution contains 20mM HEPES pH-8.0, 100mM NaCl and 20% Glycerol.

    Purity

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

    More Info

    • Introduction

      Intrinsic Factor is a member of the cobalamin transport protein family. It encodes a glycoprotein secreted by parietal cells of the gastric mucosa and is required for adequate absorption of vitamin B12 in the terminal ileum. Vitamin B12 is essential for erythrocyte maturation and mutations in the Intrinsic Factor may lead to congenital pernicious anemia. Upon entry into the stomach, vitamin B12 binds to one of two B12 binding proteins present in the gastric fluid. In the less acidic environment of the small intestine, these proteins dissociate from the vitamin, allowing it to bind to intrinsic factor and enter the portal circulation through a receptor in the ileal mucosa specific for the B12-intrinsic factor complex.

    • Synonyms

      Gastric intrinsic factor, Intrinsic factor, INF, IF, GIF, IFMH, TCN3, Cobalamin/Vitamin B-12 binding transport protein.

    • Physical Appearance

      Sterile Filtered pink solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

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    Intrinsic Factor Human
  • View Data Sheet

    Name :

    ATP1B3 Human

    Description:

    ATPaseTransporting Beta 3 Human Recombinant

    ATPase Na+/K+ Transporting Beta 3 Polypeptide, Sodium-Potassium ATPase Subunit Beta 3 (Non-Catalytic), Sodium/Potassium-Transporting ATPase Subunit Beta-3, Sodium/Potassium-Dependent ATPase Subunit Beta-3, Sodium Pump Subunit Beta-3, ATPB-3, Sodium/Potassium-Transporting ATPase Beta-3 Chain, Sodium/Potassium-Dependent ATPase Beta-3 Subunit, Na K-ATPase Beta-3 Polypeptide, CD298 Antigen, CD298, ATP1B3.

    Product # :

    PRO-1962

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    Description

    ATP1B3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (57-279) and having a molecular mass of 27.4 kDa.ATP1B3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ATP1B3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 20% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ATPaseTransporting Beta 3 (ATP1B3) is a member of the X(+)/potassium ATPases subunit beta family. ATP1B3 is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na+ and K+ ions across the plasma membrane. The beta subunit controls, by way of assembly of alpha/beta heterodimers, the quantity of sodium pumps transported to the plasma membrane. The precise role of the beta-3 subunit is unknown.

    • Synonyms

      ATPase Na+/K+ Transporting Beta 3 Polypeptide, Sodium-Potassium ATPase Subunit Beta 3 (Non-Catalytic), Sodium/Potassium-Transporting ATPase Subunit Beta-3, Sodium/Potassium-Dependent ATPase Subunit Beta-3, Sodium Pump Subunit Beta-3, ATPB-3, Sodium/Potassium-Transporting ATPase Beta-3 Chain, Sodium/Potassium-Dependent ATPase Beta-3 Subunit, Na K-ATPase Beta-3 Polypeptide, CD298 Antigen, CD298, ATP1B3.

    • 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 MGSTMWVMLQ TLNDEVPKYR DQIPSPGLMV FPKPVTALEY TFSRSDPTSY AGYIEDLKKF LKPYTLEEQK NLTVCPDGAL FEQKGPVYVA CQFPISLLQA CSGMNDPDFG YSQGNPCILV KMNRIIGLKP EGVPRIDCVS KNEDIPNVAV YPHNGMIDLK YFPYYGKKLH VGYLQPLVAV QVSFAPNNTG KEVTVECKID GSANLKSQDD RDKFLGRVMF KITARA.

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    Atp1B3 Human
  • View Data Sheet

    Name :

    ATP5H Human

    Description:

    ATP Synthase Mitochondrial Fo Complex Subunit D Human Recombinant

    ATP Synthase H+ Transporting, Mitochondrial Fo Complex Subunit D, ATP Synthase D Chain Mitochondrial, ATP Synthase H+ Transporting Mitochondrial F1F0 Subunit D, ATPase Subunit D, My032 Protein, ATPQ.

    Product # :

    PRO-1631

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    Description

    ATP5H Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (1-161) and having a molecular mass of 20.9kDa.ATP5H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ATP5H solution 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

      ATP5H is a member of the ATPase d subunit family and encodes the d subunit of the F0 complex. Electron transport complexes of the respiratory chain create a proton gradient across the membrane which induces ATP5H to transform ADP to ATP. Two alternatively spliced isoforms of ATP5H, encoded by a gene that maps to human chromosome 17q25.1, are known. ATP5H is restricted to mitochondrial inner membrane.

    • Synonyms

      ATP Synthase H+ Transporting, Mitochondrial Fo Complex Subunit D, ATP Synthase D Chain Mitochondrial, ATP Synthase H+ Transporting Mitochondrial F1F0 Subunit D, ATPase Subunit D, My032 Protein, ATPQ.

    • 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 MGSMAGRKLA LKTIDWVAFA EIIPQNQKAI ASSLKSWNET LTSRLAALPE NPPAIDWAYY KANVAKAGLV DDFEKKFNAL KVPVPEDKYT AQVDAEEKED VKSCAEWVSL SKARIVEYEK EMEKMKNLIP FDQMTIEDLN EAFPETKLDK KKYPYWPHQP IENL

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    Atp5H Human
  • View Data Sheet

    Name :

    NRG4 Human

    Description:

    Neuregulin-4 Human Recombinant

    Neuregulin 4, HRG4, Pro-neuregulin-4, membrane-bound isoform, Pro-NRG4, NRG-4.

    Product # :

    CYT-808

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    Description

    NRG4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 84 amino acids (1-61 a.a.) and having a molecular mass of 9.1kDa. NRG4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NRG4 protein solution (0.25mg/ml) contains 20mM Tris-HCl(pH8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuregulin-4 (NRG4) is a part of the neuregulin family that owns 1 EGF-like domain and is a low affinity ligand for the ERBB4 tyrosine kinase receptor. NRG4 links ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors.

    • Synonyms

      Neuregulin 4, HRG4, Pro-neuregulin-4, membrane-bound isoform, Pro-NRG4, NRG-4.

    • 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 MGSMPTDHEE PCGPSHKSFC LNGGLCYVIP TIPSPFCRCV ENYTGARCEE VFLPGSSIQT KSNL.

    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.

    Nrg4 Human
  • View Data Sheet

    Name :

    BNP Protein

    Description:

    B-type Natriuretic Peptide Human Recombinant

    NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    Product # :

    CYT-327

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    Description

    B-type Natriuretic Peptide Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 32 amino acids and having a molecular mass of 3,500 Dalton. NPPB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Natriuretic Peptide Precursor B was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      Natriuretic Peptide Precursor B acts as a cardiac hormone with a variety of biological actions including natriuresis, diuresis, vasorelaxation, and inhibition of renin and aldosterone secretion. It is thought to play a key role in cardiovascular homeostasis. Helps restore the body's salt and water balance. Improves heart function.

    • Synonyms

      NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.

    • Background

      What is the molecular weight / Mw of BNP Protein?
      BNP Protein has a total Mw of 3.5kDa.

      What is the source or expression system of BNP Protein?

      Escherichia Coli.

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

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

      What is the amino acid sequence of BNP Protein?

      SPKMVQGSGCFGRKMDRISSSSGLGCKVLRRH.

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

      What is the endotoxin level for BNP Protein?

      The endotoxin level is minimal, BNP Protein was purified using conventional chromatography techniques.

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    Nppb Human Recombinant
  • View Data Sheet

    Name :

    FABP4 Human, His

    Description:

    Fatty Acid Binding Protein 4 Human Recombinant, His Tag

    Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.

    Product # :

    PRO-566

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    Description

    FABP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 18 kDa. FABP4 is fused to His tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    FABP4 His-Tag is supplied in 20mM Tris HCL pH=8, 0.5mM DTT and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adipocyte fatty acid binding protein FABP4 is a 15 kDa member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds (bile acids or retinoids) in an internal cavity. FABP4 is expressed in a differentiation-dependent fashion in adipocytes and is a critical gene in the regulation of the biological function of these cells.
      In mice, targeted mutations in FABP4 provide significant protection from hyperinsulinemia and insulin resistance in the context of both dietary and genetic obesity. Adipocytes obtained from FABP4-deficient mice also have reduced efficiency of ipolysis in vitro and in vivo, and these mice exhibited moderately improved systemic dyslipidemia. Recent studies also demonstrated FABP4 expression in macrophages upon differentiation and activation. In these cells, FABP4 modulates inflammatory responses and cholesterol ester accumulation, and total or macrophage-specific FABP4 deficiency confers dramatic protection against atherosclerosis in the apoE-/- mice. These results indicate a central role for FABP4 in the development of major components of the metabolic syndrome through its distinct actions in adipocytes and macrophages.

    • Synonyms

      Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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.

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    Fabp4 Human His
  • View Data Sheet

    Name :

    PDIA6 Human, Active

    Description:

    Protein Disulfide Isomerase A6 Human Recombinant, Active

    Protein disulfide-isomerase A6, Endoplasmic reticulum protein 5, ER protein 5, ERp5, Protein disulfide isomerase P5, Thioredoxin domain-containing protein 7, PDIA6, ERP5, P5, TXNDC7.

    Product # :

    ENZ-994

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    Description

    PDIA6 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 442 amino acids (20-440 a.a.) and having a molecular mass of 48.5kDa. The PDIA6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PDIA6 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 10 A650/cm/min/mg. Enzymatic activity was confirmed by measuring the aggregation of INS in the presence of DTT.

    More Info

    • Introduction

      PDIA6 belongs to the protein disulfide isomerase family (PDI). PDIA6 is an enzyme in the endoplasmic reticulum in eukaryotes or periplasmic space of prokaryotes which catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. PDIA6 functions as a chaperone that inhibits aggregation of misfolded proteins. PDIA6, also has a role in platelet aggregation and activation by agonists such as convulxin, collagen and thrombin.

    • Synonyms

      Protein disulfide-isomerase A6, Endoplasmic reticulum protein 5, ER protein 5, ERp5, Protein disulfide isomerase P5, Thioredoxin domain-containing protein 7, PDIA6, ERP5, P5, TXNDC7.

    • 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 MLYSSSDDVI ELTPSNFNRE VIQSDSLWLV EFYAPWCGHC QRLTPEWKKA ATALKDVVKV GAVDADKHHS LGGQYGVQGF PTIKIFGSNK NRPEDYQGGR TGEAIVDAAL SALRQLVKDR LGGRSGGYSS GKQGRSDSSS KKDVIELTDD SFDKNVLDSE DVWMVEFYAP WCGHCKNLEP EWAAAASEVK EQTKGKVKLA AVDATVNQVL ASRYGIRGFP TIKIFQKGES PVDYDGGRTR SDIVSRALDL FSDNAPPPEL LEIINEDIAK RTCEEHQLCV VAVLPHILDT GAAGRNSYLE VLLKLADKYK KKMWGWLWTE AGAQSELETA LGIGGFGYPA MAAINARKMK FALLKGSFSE QGINEFLREL SFGRGSTAPV GGGAFPTIVE REPWDGRDGE LPVEDDIDLS DVELDDLGKD EL.

    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.

    Pdia6 Human Active
  • View Data Sheet

    Name :

    Cardiac Actin Bovine

    Description:

    Cardiac Actin Bovine

    Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.

    Product # :

    PRO-519

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    Description

    Ultra pure Cardiac Actin having a Molecular mass of 43,000 dalton.

    Source

    Bovine Heart.

    Formulation

    The protein was lyophilized from a 1mg/ml solution containing 10mM Tris-acetate buffer pH 8.0, 0.2mM CaCl2, 0.2mM ATP, 1mM DTT and 0.5% SDS.

    Purity

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

    More Info

    • Introduction

      Alpha-cardiac actin belongs to the actin family which is comprised of three main groups of actin isoforms, alpha, beta, and gamma. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. Defects in the cardiac actin have been associated with idiopathic dilated cardiomyopathy (IDC) and familial hypertrophic cardiomyopathy (FHC).

    • Synonyms

      Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

      Protein standard in 1D and 2D SDS gelelectrophoresis
      Immunoassays
      Immunization.

    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.

    Cardiac Actin
  • View Data Sheet

    Name :

    PHB Human

    Description:

    Prohibitin Human Recombinant

    PHB1, Prohibitin.

    Product # :

    PRO-1381

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    Description

    PHB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 292 amino acids (1-272a.a) and having a molecular mass of 31.9kDa. PHB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    PHB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prohibitin (PHB) is an evolutionarily conserved gene that is ubiquitously expressed and which Mutations have been linked to sporadic breast cancer. PHB is thought to be a negative regulator of cell proliferation and may be a tumor suppressor. Prohibitin is expressed as two transcripts with changeable lengths of 3' untranslated region. The longer transcript is present at higher levels in proliferating tissues and cells, proposing that this longer 3' untranslated region functions as a trans-acting regulatory RNA.

    • Synonyms

      PHB1, Prohibitin.

    • 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 MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIFTSI GEDYDERVLP SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ.

    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.

    Phb Human
  • View Data Sheet

    Name :

    FKBP2 Human

    Description:

    FK506 Binding Protein 2 Human Recombinant

    FKBP13, FKBP-2, Peptidyl-prolyl cis-trans isomerase FKBP2, PPIase FKBP2, FK506-binding protein 2, Rotamase, Immunophilin FKBP13, 13 kDa FK506-binding protein, 13 kDa FKBP, FKBP-13, FKBP2, PPIase.

    Product # :

    ENZ-503

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    Description

    FKBP2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 122 amino acids (22-142 a.a.) and having a molecular mass of 13.4 kDa. The FKBP2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FKBP2 solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 270 nmoles/min/ug, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      FKBP2 is part of the immunophilin protein family, which takes part in immunoregulation and basic cellular processes involving protein folding and trafficking. FKBP2 is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. FKBP2 functions as an ER chaperone and as a component of membrane cytoskeletal scaffolds.

    • Synonyms

      FKBP13, FKBP-2, Peptidyl-prolyl cis-trans isomerase FKBP2, PPIase FKBP2, FK506-binding protein 2, Rotamase, Immunophilin FKBP13, 13 kDa FK506-binding protein, 13 kDa FKBP, FKBP-13, FKBP2, PPIase.

    • Physical Appearance

      Sterile Filtered clear 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

      MATGAEGKRK LQIGVKKRVD HCPIKSRKGD VLHMHYTGKL EDGTEFDSSL PQNQPFVFSL GTGQVIKGWD QGLLGMCEGE KRKLVIPSEL GYGERGAPPK IPGGATLVFE VELLKIERRT EL.

    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.

    Fkbp2 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.

    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.

    Inhibin A Human
  • View Data Sheet

    Name :

    PI16 Human

    Description:

    Peptidase Inhibitor 16 Human Recombinant

    Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.

    Product # :

    ENZ-113

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    Description

    The Peptidase Inhibitor 16 Human Recombinant is produced in HEK293 cells and fused with a C-terminal Flag Tag (11 amino acids). The PI16 Flag Tagged Fusion Protein is 45.7kDa protein containing a total of 426 amino acid residues and purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    PI16 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptidase Inhibitor 16 (PI16) which a member of the CRISP family, is a putative serine protease inhibitor. PI16 interacts with PSP94/MSMB. PI16 is expressed in the prostate, testis, ovary and intestine. It also concentrates in prostate cancer patient's sera. PI16 may serve as a marker following prostatectomy for prostate cancer.

    • Synonyms

      Peptidase inhibitor 16, PI-16, Cysteine-rich secretory protein 9, CRISP-9, PSP94-binding protein, PI16, CRISP9, PSPBP, MSMBBP, MGC45378, DKFZp586B1817.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized PI16 Human recombinant 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 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.

    • Amino Acid Sequence

      LTDEEKRLMV ELHNLYRAQV SPPASDMLHM RWDEELAAFA KAYARQCVWG HNKERGRRGE NLFAITDEGM DVPLAMEEWH HEREHYNLSA ATCSPGQMCG HYTQVVWAKT ERIGCGSHFC EKLQGVEETN IELLVCNYEP PGNVKGKRPY QEGTPCSQCP SGYHCKNSLC EPIGSPEDAQ DLPYLVTEAP SFRATEASDS RKMGTPSSLA TGIPAFLVTE VSGSLATKAL PAVETQAPTS LATKDPPSMA TEAPPCVTTE VPSILAAHSL PSLDEEPVTF PKSTHVPIPK SADKVTDKTK VPSRSPENSL DPKMSLTGAR ELLPHAQEEA EAEAELPPSS EVLASVFPAQ DKPGELQATL DHTGHTSSKS LPNFPNTSAT ANATGGRALA LQSSLPGAEG PDKPSVVSGL NSGPGAAADYKDDDDK.

    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.

    Pi16 Human
  • View Data Sheet

    Name :

    KISS1 Human

    Description:

    KISS-1 Metastasis-Suppressor Human Recombinant

    Kisspeptin-1, KISS-1, METASTIN, Metastasis-suppressor KiSS-1, KISS1, MGC39258.

    Product # :

    PRO-419

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    Description

    KISS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (20-138) and having a molecular mass of 12.6 Dalton. The KISS1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KISS1 is a metastasis suppressor protein that suppresses metastases of melanomas and breast carcinomas without affecting tumorigenicity.KISS1 functions to inhibit chemotaxis and invasion, attenuating metastasis in malignant melanomas. KISS1 is involved in the regulation of cell-matrix adhesion. KISS1 plays a role in cytoskeletal reorganization. A polymorphism in the terminal exon of KISS1 mRNA results in two protein isoforms. Expression of KiSS1 is localized to specific regions of the hypothalamus in numerous species and is regulated by gonadal steroids and across the estrous cycle..KISS1 generates a c-terminally amidated peptide, metastin which functions as the endogenous ligand of the g-protein coupled receptor gpr54. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis.

    • Synonyms

      Kisspeptin-1, KISS-1, METASTIN, Metastasis-suppressor KiSS-1, KISS1, MGC39258.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MEPLEKVASV GNSRPTGQQL ESLGLLAPGE QSLPCTERKP AATARLSRRG TSLSPPPESS GSPQQPGLSA PHSRQIPAPQ GAVLVQREKD LPNYNWNSFG LRFGKREAAP GNHGRSAGRG.

    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.

    Kiss1 Human
  • View Data Sheet

    Name :

    PPIL4 Human

    Description:

    Peptidylprolyl Isomerase (Cyclophilin)-Like 4 Human Recombinant

    Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.

    Product # :

    ENZ-026

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    Description

    PPIL4 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 512 amino acids (1-492 a.a.) and having a molecular mass of 59.3kDa. The PPIL4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPIL solution (0.5 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 190 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      PPIL4 belongs to an evolutionarily conserved cyclophilin-type PPIase family of proteins. PPIL4, which is ubiquitously expressed with predominant expression in kidney localizes to the nucleus and contains one PPIase cyclophilin-type domain, a lysine-rich domain, a pair of bipartite nuclear targeting sequences and one RRM (RNA recognition motif) domain. The presence of the RRM domain along with nuclear targeting sequences implies that PPIL4 may be involved in transcriptional regulation.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase-like 4, PPIase, Cyclophilin-like protein PPIL4, Rotamase PPIL4, PPIL4, HDCME13P.

    • 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 MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD GVHTVFGEVT EGMDIIKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE PTREQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPPNLV LKDKVKPKQD TKYDLILDEQ AEDSKSSHSH TSKKHKKKTH HCSEEKEDED YMPIKNTNQD IYREMGFGHY EEEESCWEKQ KSEKRDRTQN RSRSRSRERD GHYSNSHKSK YQTDLYERER SKKRDRSRSP KKSKDKEKSK YR.

    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.

    Ppil4 Human
  • View Data Sheet

    Name :

    LILRB2 Human

    Description:

    Leukocyte Immunoglobulin Like Receptor B2 Human Recombinant

    Leukocyte Immunoglobulin-like Receptor, CD85D, CD85d, CD85 antigen-like family member D, CD85d antigen, ILT-4, ILT4, ILT4CD85d, Ig-like transcript 4, Immunoglobulin-like transcript 4, LILRB2, LIR2, LIR-2, LIR2CD85D, Leukocyte immunoglobulin-like receptor 2, MIR10, MIR-10, MIR10LILRA6, Monocyte/macrophage immunoglobulinlike receptor 10, leukocyte immunoglobulin-like receptor subfamily B member 2, leukocyte immunoglobulin-like receptor subfamily B member 2 soluble isoform 1.

    Product # :

    PRO-2729

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    Description

    LILRB2 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 444 amino acids (24-461 a.a) and having a molecular mass of 48.3kDa.LILRB2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The LILRB2 solution (0. 5mg/ml) contains phosphate buffered saline (pH7.4) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Leukocyte Immunoglobulin Like Receptor B2 (LILRB2) is a member of the leukocyte immunoglobulin-like receptor (LIR) family. LILRB2is expressed on immune cells where it binds to MHC class I molecules on antigen-presenting cells and transduces a negative signal that inhibits stimulation of an immune response.LILRB2controls inflammatory responses and cytotoxicity to help focus the immune response and limit autoreactivity.LILRB2competes with CD8 alpha for MHC I binding. LILRB2binds to classical MHC I proteins as well as the non-classical HLA-G1 and HLA-F molecules.

    • Synonyms

      Leukocyte Immunoglobulin-like Receptor, CD85D, CD85d, CD85 antigen-like family member D, CD85d antigen, ILT-4, ILT4, ILT4CD85d, Ig-like transcript 4, Immunoglobulin-like transcript 4, LILRB2, LIR2, LIR-2, LIR2CD85D, Leukocyte immunoglobulin-like receptor 2, MIR10, MIR-10, MIR10LILRA6, Monocyte/macrophage immunoglobulinlike receptor 10, leukocyte immunoglobulin-like receptor subfamily B member 2, leukocyte immunoglobulin-like receptor subfamily B member 2 soluble isoform 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

      GTIPKPTLWA EPDSVITQGS PVTLSCQGSL EAQEYRLYRE KKSASWITRI RPELVKNGQF HIPSITWEHT GRYGCQYYSR ARWSELSDPL VLVMTGAYPK PTLSAQPSPV VTSGGRVTLQ CESQVAFGGF ILCKEGEDEH PQCLNSQPHA RGSSRAIFSV GPVSPNRRWS HRCYGYDLNS PYVWSSPSDL LELLVPGVSK KPSLSVQPGP VMAPGESLTL QCVSDVGYDR FVLYKEGERD LRQLPGRQPQ AGLSQANFTL GPVSRSYGGQ YRCYGAHNLS SECSAPSDPL DILITGQIRG TPFISVQPGP TVASGENVTL LCQSWRQFHT FLLTKAGAAD APLRLRSIHE YPKYQAEFPM SPVTSAHAGT YRCYGSLNSD PYLLSHPSEP LELVVSGPSM GSSPPPTGPI STPAGPEDQP LTPTGSDPQS GLGRHLGVHH HHHH

    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.

    Lilrb2 Human
  • View Data Sheet

    Name :

    GNLY Human

    Description:

    Granulysin Human Recombinant

    LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    Product # :

    PRO-852

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    Description

    GNLY Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and fused to a double His Tag (N+C terminus) and having a total molecular mass of 18.1 kDa.The GNLY is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.

    • Synonyms

      LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHHSSGLVPRGSHMMEGLVFSRLSPEYYD
      LARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYR
      TCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWR
      DVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPS
      TGPLGSHHHHHH.

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    Gnly Human
  • View Data Sheet

    Name :

    GRPEL1 Human

    Description:

    GrpE-Like 1 Human Recombinant

    HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.

    Product # :

    PRO-263

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    • More Info

    Description

    GRPEL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (28-217a.a.) and having a molecular mass of 23.6kDa.GRPEL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GRPEL1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GRPEL1 is a vital component of the PAM complex, a complex necessary for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. GRPEL1 protein controls the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.

    • Synonyms

      HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.

    • 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 MCTATKQKNS GQNLEEDMGQ SEQKADPPAT EKTLLEEKVK LEEQLKETVE KYKRALADTE NLRQRSQKLV EEAKLYGIQA FCKDLLEVAD VLEKATQCVP KEEIKDDNPH LKNLYEGLVM TEVQIQKVFT KHGLLKLNPV GAKFDPYEHE ALFHTPVEGK EPGTVALVSK VGYKLHGRTL RPALVGVVKE A

    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.

    Grpel1 Human
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