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Search results

1000 results found for “pitpn”

Name

Description

Product #

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  • View Data Sheet

    Name :

    AAGAB Human

    Description:

    Alpha & Gamma-Adaptin Binding Protein Human Recombinant

    P34, Alpha- and gamma-adaptin-binding protein p34.

    Product # :

    PRO-1479

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    AAGAB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-315 a.a.) and having a molecular mass of 36.7kDa.AAGAB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AAGAB protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Alpha & Gamma-Adaptin Binding Protein (AAGAB), which is also known as P34, takes part in membrane traffic and interacts with AP1G1 and AP2A1.AAGAB is highly expressed in skin and keratinocytes, with the highest levels in adrenal gland, rectum and thymus.

    • Synonyms

      P34, Alpha- and gamma-adaptin-binding protein p34.

    • 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 MAAGVPCALV TSCSSVFSGD QLVQHILGTE DLIVEVTSND AVRFYPWTID NKYYSADINL CVVPNKFLVT AEIAESVQAF VVYFDSTQKS GLDSVSSWLP LAKAWLPEVM ILVCDRVSED GINRQKAQEW CIKHGFELVE LSPEELPEED DDFPESTGVK RIVQALNANV WSNVVMKNDR NQGFSLLNSL TGTNHSIGSA DPCHPEQPHL PAADSTESLS DHRGGASNTT DAQVDSIVDP MLDLDIQELA SLTTGGGDVE NFERLFSKLK EMKDKAATLP HEQRKVHAEK VAKAFWMAIG GDRDEIEGLS SDEEH.

    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.

    Aagab Human
  • View Data Sheet

    Name :

    MRPL48 Human

    Description:

    Mitochondrial Ribosomal Protein L48 Human Recombinant

    Mitochondrial Ribosomal Protein L48, MRP-L48, L48MT, 39S Ribosomal Protein L48, Mitochondrial, CGI-118, HSPC290, 39S ribosomal protein L48, mitochondrial.

    Product # :

    PRO-2099

    Price :

    Quantity :

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    • description
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    Description

    MRPL48 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (29-212 a.a) and having a molecular mass of 23.1kDa. MRPL48 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MRPL48 protein solution (1 mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mitochondrial Ribosomal Protein L48, also known as MRPL48, is a mammalian mitochondrial ribosomal protein which assists in protein synthesis within the mitochondrion. Mitochondrial ribosomes, mitoribosomes, consist of a small 28S subunit and a large 39S subunit. They include an estimated 75% protein to rRNA composition while comparing to prokaryotic ribosomes, where this ratio is reversed.An additional dissimilarity between mammalian mitoribosomes & prokaryotic ribosomes is that the latter contain a 5S rRNA. Between different species, the proteins containing the mitoribosome differ very much in sequence, as well as in biochemical properties from time to time, which prevents easy recognition through sequence homology. MRPL48 encodes a 39S subunit protein. A pseudogene corresponding to MRPL48 is found on chromosome 6p.

    • Synonyms

      Mitochondrial Ribosomal Protein L48, MRP-L48, L48MT, 39S Ribosomal Protein L48, Mitochondrial, CGI-118, HSPC290, 39S ribosomal protein L48, mitochondrial.

    • 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 MGSSGEKPIY SVGGILLSIS RPYKTKPTHG IGKYKHLIKA EEPKKKKGKV EVRAINLGTD YEYGVLNIHL TAYDMTLAES YAQYVHNLCN SLSIKVEESY AMPTKTIEVL QLQDQGSKML LDSVLTTHER VVQISGLSAT FAEIFLEIIQ SSLPEGVRLS VKEHTEEDFK GRFKARPELE ELLAKLK.

    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.

    Mrpl48 Human
  • View Data Sheet

    Name :

    DPP4 Human

    Description:

    Dipeptidyl-Peptidase 4 Human Recombinant

    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-375

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    DPPIV Human Recombinant produced in Insect cells is a single, glycosylated polypeptide chain containing 737 amino acids (39-766) and having a molecular mass of 85.4kDa.DPPIV is fused to a 6 His Tag at C-terminus and purified using conventional chromatography techniques.

    Source

    Insect cells.

    Formulation

    DPP4 is formulated in 20mM Tris-HCl buffer pH-8, 100mM NaCl, 1mM EDTA and 10% glycerol.

    Purity

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

    Biological Activity

    >200 Units/mg.

    More Info

    • Introduction

      DPP4 also called adenosine deaminase complexing protein-2, and T-cell activation antigen CD26 is a serine exopeptidase and complex enzyme that is expressed on the surface of most cell types. DPPIV is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. DPP4 plays a role in t-cell activation. DPP4 is associated with intracellular signal transduction, apoptosis and involved in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and GLP-1.

    • 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

      ADPSRKTYTL TDYLKNTYRL KLYSLRWISD HEYLYKQENN ILVFNAEYGN SSVFLENSTF DEFGHSINDY SISPDGQFIL LEYNYVKQWR HSYTASYDIY DLNKRQLITE ERIPNNTQWV TWSPVGHKLA YVWNNDIYVK IEPNLPSYRI TWTGKEDIIY NGITDWVYEE EVFSAYSALW WSPNGTFLAY AQFNDTEVPL IEYSFYSDES LQYPKTVRVP YPKAGAVNPT VKFFVVNTDS LSSVTNATSI QITAPASMLI GDHYLCDVTW ATQERISLQW LRRIQNYSVM DICDYDESSG RWNCLVARQH IEMSTTGWVG RFRPSEPHFT LDGNSFYKII SNEEGYRHIC YFQIDKKDCT FITKGTWEVI GIEALTSDYL YYISNEYKGM PGGRNLYKIQ LSDYTKVTCL SCELNPERCQ YYSVSFSKEA KYYQLRCSGP GLPLYTLHSS VNDKGLRVLE DNSALDKMLQ NVQMPSKKLD FIILNETKFW YQMILPPHFD KSKKYPLLLD VYAGPCSQKA DTVFRLNWAT YLASTENIIV ASFDGRGSGY QGDKIMHAIN RRLGTFEVED QIEAARQFSK MGFVDNKRIA IWGWSYGGYV TSMVLGSGSG VFKCGIAVAP VSRWEYYDSV YTERYMGLPT PEDNLDHYRN STVMSRAENF KQVEYLLIHG TADDNVHFQQ SAQISKALVD VGVDFQAMWY TDEDHGIASS TAHQHIYTHM SHFIKQCFSL PHHHHHH.

    • Unit Definition

      One unit will hydrolyze 1 umole of p-nitroaniline per minute at pH8.0 at 37°C using 1mM of Gly-Pro p-nitroanilde as a substrate.

    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.

    Dpp4 Human
  • View Data Sheet

    Name :

    SIRPG Human

    Description:

    Signal-Regulatory Protein Gamma Human Recombinant

    signal-regulatory protein gamma isoform 1 precursor, bA77C3.1, CD172g, SIRP-B2, SIRPB2, SIRPgamma, Signal-Regulatory Protein Gamma, SIRPG, SIRP-b2, SIRP-beta-2, CD_antigen: CD172g, CD172 antigen-like family member B, Signal-regulatory protein beta-2, SIRP-gamma.

    Product # :

    PRO-2013

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • More Info

    Description

    SIRPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (29-360 a.a.) and having a molecular mass of 39.1kDa.SIRPG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Signal-Regulatory Protein Gamma (SIRPG) belongs to the signal-regulatory protein (SIRP) family whose members are receptor-type transmembrane glycoproteins which negatively regulate the receptor tyrosine kinase-coupled signaling processes. SIRPG is also a part of the immunoglobulin superfamily.

    • Synonyms

      signal-regulatory protein gamma isoform 1 precursor, bA77C3.1, CD172g, SIRP-B2, SIRPB2, SIRPgamma, Signal-Regulatory Protein Gamma, SIRPG, SIRP-b2, SIRP-beta-2, CD_antigen: CD172g, CD172 antigen-like family member B, Signal-regulatory protein beta-2, SIRP-gamma.

    • 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 MGSEEELQMI QPEKLLLVTV GKTATLHCTV TSLLPVGPVL WFRGVGPGRE LIYNQKEGHF PRVTTVSDLT KRNNMDFSIR ISSITPADVG TYYCVKFRKG SPENVEFKSG PGTEMALGAK PSAPVVLGPA ARTTPEHTVS FTCESHGFSP RDITLKWFKN GNELSDFQTN VDPTGQSVAY SIRSTARVVL DPWDVRSQVI CEVAHVTLQG DPLRGTANLS EAIRVPPTLE VTQQPMRVGN QVNVTCQVRK FYPQSLQLTW SENGNVCQRE TASTLTENKD GTYNWTSWFL VNISDQRDDV VLTCQVKHDG QLAVSKRLAL EVTVHQKDQS SDATP.

    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.

    Sirpg Human
  • View Data Sheet

    Name :

    SNCA A30P/A53T Human

    Description:

    Alpha Synuclein A30P/A53T Human Recombinant

    Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    Product # :

    PRO-160

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    Description

    A-Synuclein A30P/A53T Human Recombinant which is a Parkinson’s disease-related double mutant, produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.5kDa (molecular size on SDS-PAGE will appear higher). The Recombinant Human a-Synuclein A30P/A53T is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SNCA A30P/A53T protein solution (1mg/ml) contains 20mM Tris-HCl buffer pH 7.5 and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      a-Synuclein (amino acids 1-140), an acidic neuronal protein of 140 amino acids, is extremely heat-resistant and is natively unfolded with an extended structure primarily composed of random coils. a-synuclein has been suggested to be implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders, and more recently, to be an important regulatory component of vesicular transport in neuronal cells. Moreover, recent studies have shown that a-synuclein has chaperone activity and that this activity is lost upon removing its C-terminal acidic tail (amino acids 96-140).

    • Synonyms

      Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.

    • 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

      MDVFMKGLSK AKEGVVAAAE KTKQGVAEAP GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.

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    Snca A30P A53T Human
  • View Data Sheet

    Name :

    GLRX3 Human

    Description:

    Glutaredoxin-3 Human Recombinant

    Glutaredoxin-3, Thioredoxin-like protein 2, PKC-interacting cousin of thioredoxin, PKC-theta-interacting protein, PKCq-interacting protein, GLRX3, PICOT, TXNL2, GRX3, GRX4, GLRX4, TXNL3, FLJ11864, bA500G10.4.

    Product # :

    ENZ-482

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    Description

    GLRX3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (1-335 a.a.) and having a molecular mass of 39.6kDa. GLRX3 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLRX3 solution containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutaredoxin belongs to the thiol-disulfide oxidoreductase family. Glutraredoxins catalyze the reversible reduction of protein-glutathionyl mixed disulfides to free sulfhydryl groups though a monothiol mechanism. Glutaredoxin-3 (GRX3) is an important protein involved in the regulation of signal transduction, for example during immune cell activation and development of cardiac hypertrophy, apparently in response to redox signals. GRX3 interacts with PRKCQ. GRX3 may have a role in the regulation the function of the thioredoxin system. GRX3 is expressed in the heart, spleen, testis and, to a lower extent, in the thymus and peripheral blood leukocytes. GRX3 is weakly expressed in lung, placenta, colon and small intestine.

    • Synonyms

      Glutaredoxin-3, Thioredoxin-like protein 2, PKC-interacting cousin of thioredoxin, PKC-theta-interacting protein, PKCq-interacting protein, GLRX3, PICOT, TXNL2, GRX3, GRX4, GLRX4, TXNL3, FLJ11864, bA500G10.4.

    • 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 MAAGAAEAAV AAVEEVGSAG QFEELLRLKA KSLLVVHFWA PWAPQCAQMN EVMAELAKEL PQVSFVKLEA EGVPEVSEKY EISSVPTFLF FKNSQKIDRL DGAHAPELTK KVQRHASSGS FLPSANEHLK EDLNLRLKKL THAAPCMLFM KGTPQEPRCG FSKQMVEILH KHNIQFSSFD IFSDEEVRQG LKAYSSWPTY PQLYVSGELI GGLDIIKELE ASEELDTICP KAPKLEERLK VLTNKASVML FMKGNKQEAK CGFSKQILEI LNSTGVEYET FDILEDEEVR QGLKAYSNWP TYPQLYVKGE LVGGLDIVKE LKENGELLPI LRGEN.

    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.

    Glrx3 Human
  • View Data Sheet

    Name :

    PON1 Human (170-232)

    Description:

    Paraoxonase-1 (170-232) Human Recombinant

    Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1.

    Product # :

    ENZ-1198

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    Description

    The PON1 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The PON1 His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 63 amino acid residues of the PON1 Human, 170-232 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized PON1 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. Product is not sterile!

      Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      PON1takes part in the detoxification of organophosphate insecticides such as parathion.

      PON1 is related to high-density lipoprotein (HDL) in the plasma and takes an important part in lipid metabolism and antioxidant defense.

      PON1 was first known for its ability to protect against oxidative stress and hydrolyze organophosphates.

      PON1 reduces oxidative stress by preventing the oxidation of lipids in LDL particles, which is extremely important in mitigating atherosclerosis and other cardiovascular diseases.

      PON1 has anti-inflammatory effects which help reduce inflammatory markers in different disease states.

      PON1 takes part in cholesterol metabolism, influencing the stability and formation of HDL particles, which are vital for lipid transport and reverse cholesterol efflux.

    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.

    Paraoxonase 1 Human
  • View Data Sheet

    Name :

    Resistin Human (64-110)

    Description:

    Resistin (64-110) Human Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.

    Product # :

    CYT-1232

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    Description

    The Resistin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Resistin His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 47 amino acid residues of the Resistin Human, 64-110 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Resistin 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. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      Human resistin is an adipokine primarily secreted by adipose tissue, mainly in response to obesity and inflammatory conditions.

      Resistin Function

      Resistin takes part in insulin resistance, which can be the cause of the development of type 2 diabetes. Resistin can also affect glucose metabolism and insulin signalling.

      Regulation

      Levels of resistin are influenced by factors such as inflammation, obesity and certain hormones. It tends to increase in conditions associated with obesity and metabolic syndrome.

      Clinical Relevance

      Elevated levels of resistin have been associated with obesity-related conditions, cardiovascular diseases, and metabolic disorders. Resisting is considered as a potential biomarker for these conditions.

      Resistin Mechanism

      Resistin promotes insulin resistance through different pathways such as the modulation of inflammatory processes and the inhibition of insulin signaling in target tissues like liver and muscle.

      Research

      Ongoing studies are exploring resistin’s role in metabolic regulation, the exact mechanisms of action of resistin and its potential as a therapeutic target for treating metabolic diseases.

      Overall, resistin is a critical factor in metabolic health, mainly in the context of diabetes and obesity.

    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.

    Resistin Human Protein
  • View Data Sheet

    Name :

    HIV-2 gp32, Biotin

    Description:

    HIV-2 gp32 Recombinant, Biotin Labeled

    Product # :

    HIV-135

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    Description

    HIV-2 gp32 Biotin Labeled recombinant- contains the full-length sequence of HIV-2 envelope immunodominant regions gp32 having a Mw of 32kDa and fused to a beta-galactosidase at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    0.01M Na2CO3, 10mM EDTA, 14mM beta-ME and 0.02% Sarcosyl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HIV-1 and HIV-2 appear to package their RNA differently. HIV-1 binds to any appropriate RNA whereas HIV-2 preferentially binds to mRNA which creates the Gag protein itself. This means that HIV-1 is better able to mutate. HIV-2 is transmitted in the same ways as HIV-1: Through exposure to bodily fluids such as blood, semen, tears and vaginal fluids.
      Immunodeficiency develops more slowly with HIV-2.
      HIV-2 is less infectious in the early stages of the virus than with HIV-1.
      The infectiousness of HIV-2 increases as the virus progresses.
      Major differences include reduced pathogenicity of HIV-2 relative to HIV-1, enhanced immune control of HIV-2 infection and often some degree of CD4-independence. Despite considerable sequence and phenotypic differences between HIV-1 and 2 envelopes, structurally they are quite similar. Both membrane-anchored proteins eventually form the 6-helix bundles from the N-terminal and C-terminal regions of the ectodomain, which is common to many viral and cellular fusion proteins and which seems to drive fusion.
      HIV-1 gp41 helical regions can form more stable 6-helix bundles than HIV-2 gp41 helical regions however HIV-2 fusion occurs at a lower threshold temperature (25°C), does not require Ca2+ in the medium, is insensitive to treatment of target cells with cytochalasin B, and is not affected by target membrane glycosphingolipid composition.

    • Physical Appearance

      Sterile filtered colorless clear solution.

    • Stability

      HIV-2 gp-32 although stable at room temperature for 3 weeks, should be stored at 4°C.

    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.

    Hiv 2 Gp 32 Biotin
  • View Data Sheet

    Name :

    GMNN Antibody

    Description:

    Geminin, Mouse Anti Human

    GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

    Product # :

    ANT-319

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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    • Introduction

      Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. G

    • Synonyms

      GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

    • Immunogen

      Anti-human Geminin mAb is derived from hybridization of mouse SP2/0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Geminin amino acids 1-209 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P2H7AT.

    • Applications

      Geminin antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1,000. Recommended starting dilution is 1:500.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      Geminin antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

    Geminin Antibody
  • View Data Sheet

    Name :

    PRPS1 Antibody

    Description:

    Phosphoribosyl Pyrophosphate Synthetase 1, Mouse Anti Human

    ARTS, CMTX5, PPRibP, PRSI, DFN2, Ribose-phosphate pyrophosphokinase 1, DFNX1, Phosphoribosyl pyrophosphate synthase I, PRS-I, PRPS1, KIAA0967.

    Product # :

    ANT-503

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    Formulation

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

    More Info

    • Introduction

      PRPS1 catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. PRPS1 catalyzes the phosphoribosylation of ribose 5-phosphate to 5-phosphoribosyl-1-pyrophosphate, which is essential for purine metabolism and nucleotide biosynthesis. Defects in PRPS1 result in phosphoribosylpyrophosphate synthetase superactivity, Charcot-Marie-Tooth disease X-linked recessive type 5 and Arts Syndrome.

    • Synonyms

      ARTS, CMTX5, PPRibP, PRSI, DFN2, Ribose-phosphate pyrophosphokinase 1, DFNX1, Phosphoribosyl pyrophosphate synthase I, PRS-I, PRPS1, KIAA0967.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PRPS1 mAb, clone PAT1E11AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PRPS1 protein 1-318 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and k light chain.

    • Clone

      PAT1E11AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      PRPS1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Prps1 Antibody
  • View Data Sheet

    Name :

    TNNT3 Human

    Description:

    Fast Skeletal Troponin T Human Recombinant

    Troponin T, fast skeletal muscle, TnTf, Beta-TnTF, Fast skeletal muscle troponin T (fTnT).

    Product # :

    PRO-2792

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    Description

    TNNT3 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 261 a.a and having a molecular mass of 30964 Dalton.

    Source

    Escherichia Coli.

    Formulation

    TNNT3 was lyophilized in 0.01M HCl, pH 2.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Troponin T, fast skeletal muscle, TnTf, Beta-TnTF, Fast skeletal muscle troponin T (fTnT).

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Fast Skeletal Troponin T although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNT3 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 TNNT3 in buffer containing 0.01M HCl, pH 2.0 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Troponin T3 Fast Skeletal Type (TNNT3) is a pivotal protein in the regulation of muscle contraction, specifically in fast-twitch skeletal muscles. The TNNT3 human recombinant, a product of cutting-edge biotechnology, offers a powerful tool to delve into the intricate molecular characteristics and multifaceted roles of this essential protein. This research aims to shed light on the molecular intricacies of TNNT3 and explore its significance beyond muscle contraction.

      At its core, TNNT3 plays a central role in the troponin complex, which orchestrates muscle contraction by modulating the interaction between actin and myosin filaments. This molecular complex regulates muscle contraction in response to calcium ions (Ca²⁺), a fundamental process underpinning skeletal muscle function. TNNT3, as a specific isoform of troponin T, contributes to the fine-tuning of muscle contractility.

      The importance of TNNT3 extends beyond its role in muscle physiology. It is primarily expressed in fast-twitch skeletal muscles responsible for rapid, forceful movements, such as sprinting and jumping. Consequently, TNNT3 is critical for the precise control of fast muscle contractions, ensuring optimal performance during activities requiring speed and power.

      Furthermore, TNNT3 has gained recognition for its potential relevance in various neuromuscular disorders. Mutations in the TNNT3 gene have been associated with congenital myopathies, highlighting its clinical significance. Investigating the structural and functional properties of TNNT3 can provide valuable insights into the molecular basis of these disorders and potentially pave the way for therapeutic interventions.

      The TNNT3 human recombinant serves as a gateway to comprehending the intricacies of this protein's molecular functions and its potential applications beyond muscle contraction. Researchers can leverage this recombinant protein to unravel TNNT3's structural properties, interactions with other muscle proteins, and its implications in neuromuscular diseases.

      This research endeavor aims to offer a comprehensive analysis of the TNNT3 human recombinant, emphasizing its molecular characteristics, functional roles in muscle contraction, and its relevance in the context of neuromuscular disorders. By exploring the multifaceted nature of TNNT3, we aspire to contribute to a deeper understanding of muscle biology and the potential development of novel therapeutic strategies.

    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.

    Tnnt3 Human
  • View Data Sheet

    Name :

    SERPINA1

    Description:

    Alpha 1 Antitrypsin Human

    Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, SERPINA1, A1AT, PI, A1A, AAT, PI1, MGC9222, PRO2275, MGC23330.

    Product # :

    PRO-456

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    Description

    SERPINA1 extracted from human serum and having a 54kDa molecular weight is purified by proprietary chromatographic techniques.

    Formulation

    SERPINA1 is 0.02M NH4HCO3.



    Purity

    Greater than 96% as determined by SDS-PAGE.

    More Info

    • Introduction

      SERPINA1 is secreted and is a serine protease inhibitor which its targets include elastase, plasmin, collagenase, thrombin, leucocytic proteases, trypsin, chymotrypsin, and plasminogen activator. Defects in SERPINA1 gene can cause emphysema or liver disease. Antral SERPINA1 expression is particularly induced by H. pylori infection. lung and prostate cancers have shown a significant increase in SERPINA1 serum levels compared with healthy controls though breast cancers did not show a significant change. SERPINA1 is an endogenous inhibitor of serine proteases and inhibits the catalytic domain of human recombinant matriptase in vitro. Rise in SERPINA1 occurs as an acute phase response to tissue necrosis and inflammation. mutations in SERPINA1 and SLC11A1 genes change the balance between elastase produced by leukocytes during phagocytosis.

    • Synonyms

      Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, SERPINA1, A1AT, PI, A1A, AAT, PI1, MGC9222, PRO2275, MGC23330.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SERPINA1 should be stored at 4°C.

    • Solubility

      It is recommended to reconstitute the lyophilized SERPINA1 in 0.15M NaCl, 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.

    Serpina1 Human
  • View Data Sheet

    Name :

    NRP1 Mouse

    Description:

    Neuropilin 1 Mouse Recombinant

    Neuropilin-1, A5 protein, CD304, Nrp1, Nrp.

    Product # :

    CYT-971

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    Description

    NRP1 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 843 amino acids (22-856 a.a.) and having a molecular mass of 94.7kDa (Migrates at 100-150kDa on SDS-PAGE under reducing conditions).NRP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    NRP1 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Neuropilin 1 (Nrp1) is a transmembrane glycoprotein which functions as a co-receptor for several extracellular ligands including class III/IV semaphorins, some isoforms of vascular endothelial growth factor and transforming growth factor beta. Nrp1 binds vascular endothelial growth factor (VEGF)-A and is believed to serve as a coreceptor for kinase insert domain-containing receptor (KDR) by connecting with KDR and enhancing VEGF signaling. Nrp1 is a marker of regulatory T cells.

    • Synonyms

      Neuropilin-1, A5 protein, CD304, Nrp1, Nrp.

    • 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

      FRSDKCGGTI KIENPGYLTS PGYPHSYHPS EKCEWLIQAP EPYQRIMINF NPHFDLEDRD CKYDYVEVID GENEGGRLWG KFCGKIAPSP VVSSGPFLFI KFVSDYETHG AGFSIRYEIF KRGPECSQNY TAPTGVIKSP GFPEKYPNSL ECTYIIFAPK MSEIILEFES FDLEQDSNPP GGMFCRYDRL EIWDGFPEVG PHIGRYCGQK TPGRIRSSSG VLSMVFYTDS AIAKEGFSAN YSVLQSSISE DFKCMEALGM ESGEIHSDQITASSQYGTNW SVERSRLNYP ENGWTPGEDS YKEWIQVDLG LLRFVTAVGT QGAISKETKK KYYVKTYRVD ISSNGEDWIS LKEGNKAIIF QGNTNPTDVV LGVFSKPLIT RFVRIKPVSW ETGISMRFEV YGCKITDYPC SGMLGMVSGL ISDSQITASN QADRNWMPEN IRLVTSRTGW ALPPSPHPYT NEWLQVDLGD EKIVRGVIIQ GGKHRENKVF MRKFKIAYSN NGSDWKTIMD DSKRKAKSFE GNNNYDTPEL RTFSPLSTRF IRIYPERATH SGLGLRMELL GCEVEAPTAG PTTPNGNPVD ECDDDQANCH SGTGDDFQLT GGTTVLATEK PTIIDSTIQS EFPTYGFNCE FGWGSHKTFC HWEHDSHAQL RWSVLTSKTG PIQDHTGDGN FIYSQADENQ KGKVARLVSP VVYSQSSAHC MTFWYHMSGS HVGTLRVKLR YQKPEEYDQL VWMVVGHQGD HWKEGRVLLH KSLKLYQVIF EGEIGKGNLG GIAVDDISIN NHISQEDCAK PTDLDKKNTE IKIDETGSTP GYEGEGEGDK NISRKPGNVL KTLDPLEHHH HHH

    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.

    Nrp1 Mouse
  • View Data Sheet

    Name :

    IL 22 Mouse, PEG

    Description:

    Interleukin-22 Mouse Recombinant, Pegylated

    IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

    Product # :

    CYT-701

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    Description

    Pegylated Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 147 amino acids and an aditional Ala amino acid at N-terminus having a molecular mass of 36 kDa as determioned by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as a 50 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. The Murine IL-22 is Mono-pegylated (with 20 kDa PEG) purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated solution at 0.65mg/ml containing 0.003mM NaHCO3.

    Purity

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

    Biological Activity

    The ED50 as determined by STAT3 phosphorylation assay in HepG cells. The activity in vitro was found to be ~ 10% compared to the non-pegylated mouse IL22.

    More Info

    • Introduction

      Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10Rβ (previously known as CRF2-4), belonging to the class II cytokine recep

    • Synonyms

      IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized pegylated murine IL22 although stable at room temperature for several days, should be stored desiccated below -20°C. Upon reconstitution at 0.1mg/ml pegylated mouse IL22 and up to 2mg/ml, filter and sterilized, the protein can be stored at 4 degrees Celsius for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized pegylated mouse Interleukin -22 in sterile 0.4% NaHCO3 adjusted to pH 8-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Il 22 Mouse Pegylated
  • View Data Sheet

    Name :

    CoV-2 N (196 a.a.)

    Description:

    Coronavirus 2019 Nucleocapsid (196 a.a.), Recombinant

    Product # :

    SARS-042

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    Description

    The E.Coli derived recombinant protein contains the Coronavirus 2019 middle region a.a. from the Nucleocapsid protein and fused to GST-6xHis tag at N-terminal and having a Mw. Of 48.4 kDa.

    Source

    E.Coli.

    Formulation

    CoV-2 Nucleocapsid protein solution is supplied in 50mM Tris-HCl pH 8, 1M Urea, and 50% Glycerol.

    Purity

    CoV-2 Nucleocapsid protein is >95% pure as determined SDS-PAGE.

    More Info

    • Introduction

      A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

      The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

      While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      CoV-2 Spike Protein is shipped on ice packs. Upon arrival, Store at -20°C.

    • Purification Method

      NTA Sepharose-Affinity Purification.

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

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  • View Data Sheet

    Name :

    CRTAP Human

    Description:

    Cartilage Associated Protein Human Recombinant

    CASP, LEPREL3, OI7, Cartilage-associated protein, CRTAP.

    Product # :

    PRO-1862

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    Description

    CRTAP Human Recombinant produced in E. coli is. a single polypeptide chain containing 398 amino acids (27-401) and having a molecular mass of 46.4kDa. CRTAP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cartilage-associated protein (CRTAP) is a secreted protein localizing to the extracellular space which takes part in collagen post-translational modifications, extracellular fibril assembly and intracellular trafficking. CRTAP which is mainly expressed with predominant expression in articular chondrocytes is essential for efficient 3-hydroxylation of fibrillar collagen prolyl residues. Mutations in the gene encoding CRTAP might cause to autosomal recessive osteogenesis imperfecta (OI) type 7 and type 2B.

    • Synonyms

      CASP, LEPREL3, OI7, Cartilage-associated protein, CRTAP.

    • 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 MGSQYERYSF RSFPRDELMP LESAYRHALD KYSGEHWAES VGYLEISLRL HRLLRDSEAF CHRNCSAAPQ PEPAAGLASY PELRLFGGLL RRAHCLKRCK QGLPAFRQSQ PSREVLADFQ RREPYKFLQF AYFKANNLPK AIAAAHTFLL KHPDDEMMKR NMAYYKSLPG AEDYIKDLET KSYESLFIRA VRAYNGENWR TSITDMELAL PDFFKAFYEC LAACEGSREI KDFKDFYLSI ADHYVEVLEC KIQCEENLTP VIGGYPVEKF VATMYHYLQF AYYKLNDLKN AAPCAVSYLL FDQNDKVMQQ NLVYYQYHRD TWGLSDEHFQ PRPEAVQFFN VTTLQKELYD FAKENIMDDD EGEVVEYVDD LLELEETS.

    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.

    Crtap Human
  • View Data Sheet

    Name :

    PDCL Human

    Description:

    Phosducin-Like Human Recombinant

    Phosducin-like protein, PHLP, DKFZp564M1863.

    Product # :

    PRO-1141

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    Description

    PDCL Human Recombinant produced in E. coli is a single polypeptide chain containing 325 amino acids (1-301) and having a molecular mass of 36.8 kDa.PDCL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PDCL solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosducin-like protein (PDCL) is a member of the phosducin family. PDCL is a putative modulator of heterotrimeric G proteins. PDCL shares broad amino acid sequence homology with phosducin, a phosphoprotein expressed in the retina and pineal gland. Both PDCL and phosphoducin regulate G-protein signaling by binding to the beta-gamma subunits of G proteins.

    • Synonyms

      Phosducin-like protein, PHLP, DKFZp564M1863.

    • 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 MGSHMTTLDD KLLGEKLQYY YSSSEDEDSD HEDKDRGRCA PASSSVPAEA ELAGEGISVN TGPKGVINDW RRFKQLETEQ REEQCREMER LIKKLSMTCR SHLDEEEEQQ KQKDLQEKIS GKMTLKEFAI MNEDQDDEEF LQQYRKQRME EMRQQLHKGP QFKQVFEISS GEGFLDMIDK EQKSIVIMVH IYEDGIPGTE AMNGCMICLA AEYPAVKFCK VKSSVIGASS QFTRNALPAL LIYKGGELIG NFVRVTDQLG DDFFAVDLEA FLQEFGLLPE KEVLVLTSVR NSATCHSEDS DLEID

    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.

    Pdcl Human
  • View Data Sheet

    Name :

    IFN a 2b Human

    Description:

    IFN-Alpha 2b Human Recombinant

    IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.

    Product # :

    CYT-205

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    Description

    IFN-a 2b Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 166 amino acids and having a molecular mass of 19400 Dalton. The difference between IFNA2A and IFNA2B is in the amino acid present at position 23. IFN-alpha 2a has a lysine at that position 23 while IFN-alpha 2b has arginine. The IFN-alpha 2b gene was obtained from human leukocytes. The IFN-a 2b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a (1 mg/ml) solution in containing 2.3 mg Sodium phosphate dibasic and 0.55 mg sodium phosphate monobasic buffer.

    Purity

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

    Biological Activity

    The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

    More Info

    • Introduction

      IFN-alpha is produced by macrophages and has antiviral activities. IFN stimulates the production of two enzymes: protein kinase and an oligoadenylate synthetase.

    • Synonyms

      IFN alpha 2b, IFNA, INFA2, MGC125764, MGC125765.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN alpha 2b 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 IFN-alpha 2b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE

    • Background

      IFN-alpha forms are produced by monocytes/macrophages, lymphoblastoid cells, fibroblasts, and a number of different cell types following induction by viruses, nucleic acids, glucocorticoid hormones, and low-molecular weight substances (n-butyrate, 5-bromodeoxy uridine). At least 23 different variants of IFN-alpha are known. The individual proteins have molecular masses between 19-26 kDa and consist of proteins with lengths of 156-166 and 172 amino acids. All IFN-alpha subtypes possess a common conserved sequence region between amino acid positions 115-151 while the amino-terminal ends are variable. Many IFN-alpha subtypes differ in their sequences at only one or two positions. Naturally occurring variants also include proteins truncated by 10 amino acids at the carboxy-terminal end. Disulfide bonds are formed between cysteines at positions 1/98 and 29/138. The disulfide bond 29/138 is essential for biological activity while the 1/98 bond can be reduces without affecting biological activity. All IFN-alpha forms contain a potential glycosylation site but most subtypes are not glycosylated. In contrast to IFN-gamma IFN-alpha proteins are stable at pH2.

      There are at least 23 different IFN-alpha genes. They have a length of 1-2 kb and are clustered on human chromosome 9p22. It is not known whether all these genes are expressed following stimulation of the cells. In some cell systems expression of some subtypes (IFN-alpha-1, IFN-alpha-2, IFN-alpha-4) is stronger than those of others. IFN-alpha genes do not contain intron sequences found in many other eukaryotic genes (see also: gene expression). Based upon the structures two types of IFN-alpha genes, designated class 1 and II, are distinguished. They encode proteins of 156-166 and172 amino acids, respectively. Deletions covering 9p22 are observed frequently in cells of lymphoblastoid leukemias. It is not known to date whether this is of significance with respect to IFN expression.

      The gene encoding the IFN-alpha receptor maps to human chromosome 21q22.1. IFN-alpha and IFN-beta are thought to bind to the same IFN binding subunit which is expressed in 100-5000 copies in IFN-alpha sensitive and -resistant cells and is associated with other as yet unidentified proteins. The IFN-omega (Omega IFN) also binds to the IFN-alpha/IFN-beta receptor. Another receptor expressed on B-lymphocytes is identical with CD21. This receptor also binds Epstein-Barr virus through its gp350/220 coat protein.Signal transduction mechanisms elicited after binding of IFN-alpha to its receptors involves tyrosine phosphorylation (see also: PTK; protein tyrosine kinase) of various non-receptor tyrosine kinases belonging to the Janus kinases. Soluble forms of the IFN-alpha receptor, corresponding to truncated forms of the extracellular domain of the cell surface IFN-alpha receptor, have been found in human serum and in normal human urine.

      All known subtypes of IFN-alpha show the same antiviral antiparasitic, antiproliferative activities in suitable bioassays although they may differ in relative activities. Human IFN-alpha is also a potent antiviral substance in murine, porcine, and bovine cell systems. Human IFN-alpha is less active in rodent cells. Site-directed mutagenesis techniques have been used to create some variants of certain subtypes (IFN-alpha-2) that display approximately 100-fold enhanced antiviral activities in mouse cells.

      What is the molecular weight/Mw of IFN A 2B HUMAN Protein?
      IFN A 2B HUMAN Protein has a total Mw of 19.4kDa.

      What is the source or expression system of IFN A 2B HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IFN A 2B HUMAN Protein?
      IFN A 2B HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFN A 2B HUMAN Protein?
      The specific activity as determined in a viral resistance assay using bovine kidney MDBK cells was found to be 260,000,000 IU/ mg.

      What is the amino acid sequence of IFN A 2B HUMAN Protein?
      MCDLPQTHSL GSRRTLMLLA QMRRISLFSC LKDRHDFGFP QEEFGNQFQK AETIPVLHEM IQQIFNLFST KDSSAAWDET LLDKFYTELY QQLNDLEACV IQGVGVTETP LMKEDSILAV RKYFQRITLY LKEKKYSPCA WEVVRAEIMR SFSLSTNLQE SLRSKE
      What applications can IFN A 2B HUMAN Protein be used in?
      IFN A 2B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFN A 2B HUMAN Protein?
      The endotoxin level is minimal, IFN A 2B HUMAN Protein was purified using conventional chromatography techniques.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.924 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IFN alpha 2b as a Reference Standard.

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

    Interferon Alpha 2B Human
  • View Data Sheet

    Name :

    CoV-2 N (1-419)

    Description:

    Coronavirus 2019 Nucleocapsid (1-419 a.a.), Recombinant

    Product # :

    SARS-040

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    • More Info

    Description

    The E.Colie derived recombinant protein contains the Coronavirus 2019 CoV-2 Nucleocapsid Phosphoprotein, Wuhan-Hu-1 strain, amino acids (1-419) having a Mw of 46.4 kDa and fused to 6xHis tag at C-terminal.

    Source

    E.Coli

    Formulation

    CoV-2 Nucleocapsid phosphoprotein was lyophilized from 20mM Na-carbonate buffer pH-9.2

    Purity

    Protein is >95% pure as determined SDS-PAGE.

    More Info

    • Introduction

      A human infecting coronavirus (viral pneumonia) called 2019 novel coronavirus, 2019-nCoV was found in the fish market at the city of Wuhan, Hubei province of China on December 2019.

      The 2019-nCoV shares an 87% identity to the 2 bat-derived severe acute respiratory syndrome 2018 SARS-CoV-2 located in Zhoushan of eastern China. 2019-nCoV has an analogous receptor-BD-structure to that of 2018 SARS-CoV, even though there is a.a. diversity so thus the 2019-nCoV might bind to ACE2 receptor protein (angiotensin-converting enzyme 2) in humans.

      While bats are possibly the host of 2019-nCoV, researchers suspect that animal from the ocean sold at the seafood market was an intermediate host. RSCU analysis proposes that the 2019-nCoV is a recombinant within the viral spike glycoprotein between the bat coronavirus and an unknown coronavirus.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Cov-2 Nucleocapsid phosphoprotein is shipped lyophilized at ambient temp. Although stable at room temperature for 2 weeks, should be stored desiccated below -18°C. Upon reconstitution COV2 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 CoV-2 protein in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Antigen Amino Acid Sequence

      MSDNGPQNQRNAPRITFGGPSDSTGSNQNGERSGARSKQRRPQGLPNNTASWFTALTQHGKED LKFPRGQGVPINTNSSPDDQIGYYRRATRRIRGGDGKMKDLSPRWYFYYLGTGPEAGLPYGANK DGIIWVATEGALNTPKDHIGTRNPANNAAIVLQLPQGTTLPKGFYAEGSRGGSQASSRSSSRSRN SSRNSTPGSSRGTSPARMAGNGGDAALALLLLDRLNQLESKMSGKGQQQQGQTVTKKSAAEAS KKPRQKRTATKAYNVTQAFGRRGPEQTQGNFGDQELIRQGTDYKHWPQIAQFAPSASAFFGMSR IGMEVTPSGTWLTYTGAIKLDDKDPNFKDQVILLNKHIDAYKTFPPTEPKKDKKKKADETQALPQR QKKQQTVTLLPAADLDDFSKQLQQSMSSADSTQAHHHHHH

    • Purification Method

      Purified by Metal-Afinity chromatographic technique.

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

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  • View Data Sheet

    Name :

    Leptin Rat, PEG

    Description:

    Pegylated Rat Leptin Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-592

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    Description

    Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa (with 20 kDa PEG) as determined by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

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

    Biological Activity

    Pegylated Rat Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized pegylated Rat Leptin Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution of pegylated Rat Leptin at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Rat leptin can be stored at 4C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized pegylated Rat Leptin in sterile water or in sterile 0.4% NaHCO3 adjusted to pH-8.5, not less than 100µg/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.

    Leptin Rat Pegylated
  • View Data Sheet

    Name :

    TIGIT Human

    Description:

    T-Cell Immunoreceptor With Ig And ITIM Domains Human Recombinant

    VSIG9, VSTM3, WUCAM, V-set and immunoglobulin domain-containing protein 9, V-set and transmembrane domain-containing protein 3.

    Product # :

    PRO-2498

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    Description

    TIGIT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 359 amino acids (22-141a.a.) and having a molecular mass of 40.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TIGIT is expressed with a 239 amino acid hlgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TIGIT protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      T cell immunoreceptor with Ig and ITIM domains or TIGIT, is an immune receptor located on part of T cells and Natural Killer Cells(NK). TIGIT is also known as Vstm3 and WUCAM. The receptor can bind with high affinity to dendritic cells(DCs), CD155(PVR) on macrophages, etc., and it can bind with lower affinity to CD112(PVRL2). TIGIT can inhibit the cytotoxicity of Natural Killer Cells through its ITIM domain via antibodies against the interaction with PVR and the activity is directed. It has been show on research that TIGIT-Fc fusion molecule can have interaction with PVR on dendritic cells and elevate its IL-10 secretion level or lower the secretion on IL-12 under the stimulation of LPS, moreover, it can inhibit the activation of T cell in vivo.

    • Synonyms

      VSIG9, VSTM3, WUCAM, V-set and immunoglobulin domain-containing protein 9, V-set and transmembrane domain-containing protein 3.

    • 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

      MMTGTIETTG NISAEKGGSI ILQCHLSSTT AQVTQVNWEQ QDQLLAICNA DLGWHISPSF KDRVAPGPGL GLTLQSLTVN DTGEYFCIYH TYPDGTYTGR IFLEVLESSV AEHGARFQIP LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN HYTQKSLSLS PGKHHHHHH.

    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.

    Tigit Human
  • View Data Sheet

    Name :

    GP2 Human

    Description:

    Glycoprotein-2 Human Recombinant

    Glycoprotein 2 (zymogen granule membrane), Pancreatic zymogen granule membrane protein GP-2, ZAP75, DKFZp779K0533.

    Product # :

    PRO-115

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    • source
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    • More Info

    Description

    GP2 is a cDNA coding for the free form of the human pancreatic secretory granule membrane major glycoprotein / GP2 having a molecular mass of 68,000 Dalton (protein component excluding glycosylation; observed molecular weight approx. 68 kDa) pH 5.4. GP2 protein is fused to a deca-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    GP2 solution is supplied in 16mM HEPES buffer pH-7.5, 80mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Crohn's Disease (CD), which is very common in Caucasians, is an inflammatory bowel diseases (IBD). Mucosal inflammation in CD seems to arise when dysregulation of the immune system breaks the balance between tolerance to commensal microbiota or food-derived antigens and immunity to pathogens. The autoimmune mechanisms takes part in the development of CD, and exocrine pancreas autoantibodies (PAB) are disease-specific in CD patients. It was established not too long ago that glycoprotein 2 (GP2) is the major autoantigenic mark recognized by CD-specific PAB. Furthermore to IgG and IgM PAB isotypes, IgA pancreatic autoantibodies were also identified in CD patients. GP2 is an extremely glycosylated 78 kDa protein with N-linked carbohydrates. It is responsible for up to 40% of all zymogen granule (ZG) membrane proteins in pancreatic acinar cells and is linked to the ZG membrane via a glycosyl phosphoinositol (GPI) anchor.

    • Synonyms

      Glycoprotein 2 (zymogen granule membrane), Pancreatic zymogen granule membrane protein GP-2, ZAP75, DKFZp779K0533.

    • 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.

    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.

    Gp2 Human
  • View Data Sheet

    Name :

    SAMSN1 Human

    Description:

    SAM Domain SH3 Domain and Nuclear Localization Signal 1 Human Recombinant

    HACS1, NASH1, SASH2, SH3D6B, SLy2, SAM domain-containing protein SAMSN-1, Hematopoietic adaptor containing SH3 and SAM domains 1, Nash1, SAM domain, SH3 domain and nuclear localization signals protein 1, SH3-SAM adaptor protein, SAMSN1.

    Product # :

    PRO-1995

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    Description

    SAMSN1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373a.a) and having a molecular mass of 44.1kDa. SAMSN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SAMSN1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SAM Domain SH3 Domain and Nuclear Localization Signal 1 (SAMSN1) is a member of a known adaptors and scaffold proteins containing SH3 and SAM (sterile alpha motif) domains. SAMSN1 is a negative regulator of B-cell activation and is down-regulates cell proliferation. SAMSN1 is up-regulated by IL-4 in activated B cells and expressed mainly in dendritic cells. SAMSN1 owns a function which is similar to other adaptor proteins that link signaling molecules in signal transduction cascades.

    • Synonyms

      HACS1, NASH1, SASH2, SH3D6B, SLy2, SAM domain-containing protein SAMSN-1, Hematopoietic adaptor containing SH3 and SAM domains 1, Nash1, SAM domain, SH3 domain and nuclear localization signals protein 1, SH3-SAM adaptor protein, SAMSN1.

    • 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 MGSMLKRKPS NVSEKEKHQK PKRSSSFGNF DRFRNNSLSK PDDSTEAHEG DPTNGSGEQS KTSNNGGGLG KKMRAISWTM KKKVGKKYIK ALSEEKDEED GENAHPYRNS DPVIGTHTEK VSLKASDSMD SLYSGQSSSS GITSCSDGTS NRDSFRLDDD GPYSGPFCGR ARVHTDFTPS PYDTDSLKIK KGDIIDIICK TPMGMWTGML NNKVGNFKFI YVDVISEEEA APKKIKANRR SNSKKSKTLQ EFLERIHLQE YTSTLLLNGY ETLEDLKDIK ESHLIELNIE NPDDRRRLLS AAENFLEEEI IQEQENEPEP LSLSSDISLN KSQLDDCPRD SGCYISSGNS DNGKEDLESE NLSDMVHKII ITEPSD.

    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.

    Samsn1 Human
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