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Search results

1000 results found for “albumin”

Name

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  • View Data Sheet

    Name :

    Globular Adiponectin Human

    Description:

    Globular Adiponectin Human Recombinant

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-615

    Price :

    Quantity :

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    • source
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    • purity
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    Description

    gAcrp30 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 145 amino acids and having a molecular mass of 16.7kDa. The gAcrp30 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Sterile filtered and lyophilized from 10mM sodium phosphate & 0.5mM DTT, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 669ng/ml, corresponding to a specific activity of 1.5x103units/mg.

    Citations

    More Info

    • Introduction

      gAcrp30 globular protein, exists as a result of proteolytic processing of adiponectin. Adiponectin is manufactured and secreted solely by adipocytes, and is a highly obtained plasma protein, accounting for up to 0.05% of total serum protein. Similar to Adiponectin, gAcrp30 is able of lowering hyperglycemia and reversing INS resistance. In addition, gAcrp30 is an significant protein that is involved in promoting fat loss by signaling muscle to absorb and burn Free-Fatty Acids. AdipoR1 & AdipoR2 are the 2 signaling receptors for adiponectin and gAcrp30 that were recently been identified.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Stability

      For long term, store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time two weeks.

    • Solubility

      We recommended reconstituting gAcrp30 at a concentration of 0.1mg per ml with 10mM sodium phosphate & 0.5mM DTT, pH 7.5. which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 16.7kDa.

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

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

      What is the Biological Activity of ADIPONECTIN Protein?
      gAcrp30 activity is determined by its ability to inhibit the proliferation of mouse M1 cells. The expected ED50 for this effect is 669ng/ml, corresponding to a specific activity of 1.5x103units/mg.

      What is the amino acid sequence of ADIPONECTIN Protein?
      MKGEPGEGAY VYRSAFSVGL ETYVTIPNMP IRFTKIFYNQ QNHYDGSTGK FHCNIPGLYY FAYHITVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTN.

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

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

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

    Globular Adiponectin Human
  • View Data Sheet

    Name :

    Clusterin Human, His

    Description:

    Apolipoprotein-J Human Recombinant, His Tag

    CLI, AAG4, APOJ, KUB1, SGP2, SGP-2, SP-40, TRPM2, TRPM-2, MGC24903, Clusterin, ging-associated gene 4 protein, Apolipoprotein J,Complement cytolysis inhibitor, Complement-associated protein SP-40,40, Ku70-binding protein 1, NA1/NA2, Testosterone-repressed prostate message 2, CLU.

    Product # :

    CYT-814

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • More Info
    • sds-page
    • Citations

    Description

    Clusterin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 463 amino acids (23-449 a.a.) and having a molecular mass of 54.1kDa. Clusterin is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    Clusterin-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
      Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, APOJ, KUB1, SGP2, SGP-2, SP-40, TRPM2, TRPM-2, MGC24903, Clusterin, ging-associated gene 4 protein, Apolipoprotein J,Complement cytolysis inhibitor, Complement-associated protein SP-40,40, Ku70-binding protein 1, NA1/NA2, Testosterone-repressed prostate message 2, CLU.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSDQTV SDNELQEMSN QGSKYVNKEI QNAVNGVKQI KTLIEKTNEE RKTLLSNLEE AKKKKEDALN ETRESETKLK ELPGVCNETM MALWEECKPC LKQTCMKFYA RVCRSGSGLV GRQLEEFLNQ SSPFYFWMNG DRIDSLLEND RQQTHMLDVM QDHFSRASSI IDELFQDRFF TREPQDTYHY LPFSLPHRRP HFFFPKSRIV RSLMPFSPYE PLNFHAMFQP FLEMIHEAQQ AMDIHFHSPA FQHPPTEFIR EGDDDRTVCR EIRHNSTGCL RMKDQCDKCR EILSVDCSTN NPSQAKLRRE LDESLQVAER LTRKYNELLK SYQWKMLNTS SLLEQLNEQF NWVSRLANLT QGEDQYYLRV TTVASHTSDS DVPSGVTEVV VKLFDSDPIT VTVPVEVSRK NPKFMETVAE KALQEYRKKH REE.

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 54.1kDa.

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

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

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

      What is the amino acid sequence of CLUSTERIN Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSDQTV SDNELQEMSN QGSKYVNKEI QNAVNGVKQI KTLIEKTNEE RKTLLSNLEE AKKKKEDALN ETRESETKLK ELPGVCNETM MALWEECKPC LKQTCMKFYA RVCRSGSGLV GRQLEEFLNQ SSPFYFWMNG DRIDSLLEND RQQTHMLDVM QDHFSRASSI IDELFQDRFF TREPQDTYHY LPFSLPHRRP HFFFPKSRIV RSLMPFSPYE PLNFHAMFQP FLEMIHEAQQ AMDIHFHSPA FQHPPTEFIR EGDDDRTVCR EIRHNSTGCL RMKDQCDKCR EILSVDCSTN NPSQAKLRRE LDESLQVAER LTRKYNELLK SYQWKMLNTS SLLEQLNEQF NWVSRLANLT QGEDQYYLRV TTVASHTSDS DVPSGVTEVV VKLFDSDPIT VTVPVEVSRK NPKFMETVAE KALQEYRKKH REE.

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

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

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

    Clusterin Human His
  • View Data Sheet

    Name :

    Ara h 2.0201

    Description:

    Allergen Ara h 2.0201 (Conglutin-7) Recombinant

    Conglutin-7, 2S protein 1, Seed storage protein SSP1, Seed storage protein SSP2, Allergen Ara h 2.

    Product # :

    ALR-007

    Price :

    Quantity :

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    Description

    Recombinant Allergen Ara h 2.0201 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 20,000 Dalton. Ara h 2.0201 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Ara h 2.0201 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ara h 2 comprises of 2 isoforms: Ara h 2.0101 and Ara h 2.0201. Ara h 2.0201 is the most important peanut allergen which binds IgE. Ara h 2.0201 is a Weak inhibitor of trypsin and is a conglutin storage protein which accounts together with Ara h 6.0101 for the majority of the IgE immune response.

    • Synonyms

      Conglutin-7, 2S protein 1, Seed storage protein SSP1, Seed storage protein SSP2, Allergen Ara h 2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

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

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

    Ara H 20201
  • View Data Sheet

    Name :

    Clusterin Mouse

    Description:

    Apolipoprotein-J Mouse Recombinant

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

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    CYT-1172

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    Description

    Clusterin Mouse Recombinant is a single, glycosylated polypeptide chain containing 433 amino acids (22-448a.a) and having a molecular mass of 50.2kDa (calculated). Clusterin is fused to a 6 a.a His tag at C-terminal.

    Source

    HEK293

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Clusterin also known as Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by 5 disulfide bridges and are flanked by 2 predicted coiled-coil a-helices and 3 predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% -80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, heparin, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      Clusterin is up/down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 50.2kDa.

      What is the source or expression system of CLUSTERIN Protein?
      HEK293

      What is the Purity of CLUSTERIN Protein?
      CLUSTERIN Protein is >90% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of CLUSTERIN Protein?
      EQEVSDNELQ ELSTQGSRYI NKEIQNAVQG VKHIKTLIEK TNAERKSLLN SLEEAKKKKE DALEDTRDSE MKLKAFPEVC NETMMALWEE CKPCLKHTCM KFYARVCRSG SGLVGQQLEE FLNQSSPFYF WMNGDRIDSL LESDRQQSQV LDAMQDSFAR ASGIIDTLFQ DRFFARELHD PHYFSPIGFP HKRPHFLYPK SRLVRSLMSP SHYGPPSFHN MFQPFFEMIH QAQQAMDVQL HSPAFQFPDV DFLREGEDDR TVCKEIRRNS TGCLKMKGQC EKCQEILSVD CSTNNPAQAN LRQELNDSLQ VAERLTEQYK ELLQSFQSKM LNTSSLLEQL NDQFNWVSQL ANLTQGEDKY YLRVSTVTTH SSDSEVPSRV TEVVVKLFDS DPITVVLPEE VSKDNPKFMD TVAEKALQEY RRKSRAEHHH HHH

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

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

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

    Clusterin Mouse
  • View Data Sheet

    Name :

    MAPT Human 383a.a.

    Description:

    Microtubule-Associated Protein Tau 383 a.a. Human Recombinant

    Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

    Product # :

    PRO-012

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    Description

    MAPT Human Recombinant (Isoform 3) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 403 amino acids (1-383 a.a.) and having a molecular mass of 42.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MAPT is a neuronal microtubule associated protein localized mostly on axons.
      MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain.

    • Synonyms

      Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

    • 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

      MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL.

    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.

    Mapt Human 383Aa
  • View Data Sheet

    Name :

    ENHO Human

    Description:

    Energy Homeostasis Associated Human Recombinant

    Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

    Product # :

    PRO-1569

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    Description

    ENHO Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 34-76) containing 121 amino acids including extra 78 N-terminal amino acids. The total molecular mass is 13.05kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    ENHO filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Energy Homeostasis Associated (ENHO) participates in glucose homeostasis maintenance and lipid metabolism. ENHO is expressed in the liver and the brain. The role of ENHO in obesity or diabetes is studied.

    • Synonyms

      Adropin, Energy homeostasis-associated protein, ENHO, C9orf165, UNQ470.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Amino Acid Sequence

      MGGKSNGEKK YIVGFKQGFK SCAKKEDVIS EKGGKLQKCF KYVDAASATL NEKAVEELKK DPSVAYVEED KLFKALTSCHSRSADVDSLS ESSPNSSPGP CPEKAPPPQK PSHEGSYLLQ P.

    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.

    Enho Human
  • View Data Sheet

    Name :

    Bivalirudin

    Description:

    Bivalirudin

    Product # :

    PRO-357

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    Description

    The active of Bivalirudin substance is a synthetic 20 amino acid peptide. The amino acid sequence is Phe-Pro-Arg-Pro-Gly-Gly-Gly-Gly- Asn-Gly-Asp-Phe-Glu-Glu-Ile- Pro-Glu-Glu-Tyr-Leu. The Mw is 2180 dalton.

    Formulation

    The protein (1mg/ml) was lyophilized with 0.5mg Manntiol and sodium hydroxide 50µg pH-5.5.

    Purity

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

    Citations

    More Info

    • Introduction

      Bivalirudin directly inhibits thrombin by specifically binding as well to the catalytic site and to the anion-binding exosite of circulating and clot-bound thrombin. Bivalirudin is a specific and reversible direct thrombin inhibitor.
      Thrombin, which is a serine protease, plays a central role in the thrombotic process; it cleaves fibrinogen into fibrin monomers and activates Factor XIII to Factor XIIIa, allowing fibrin to develop a covalently cross-linked structure which stabilizes the thrombus. Thrombin also activates Factors V and VIII, which promotes further thrombin generation, activates platelets, stimulating aggregation and granule release.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bivalirudin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bivalirudin 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 Bivalirudin in sterile 18MΩ-cm H2O 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.

    Bivalirudin
  • View Data Sheet

    Name :

    Adiponectin Rat

    Description:

    Adiponectin Rat Recombinant

    Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30kDa protein, Adipose most abundant gene transcript 1 protein, gelatin-binding protein, Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-831

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    Description

    ACRP30 Rat Recombinant produced in 293 cell line is a polypeptide chain containing 238 amino acids and having a total molecular mass of 25.7 kDa. ACRP30 contains a C-Terminal linker (3 AA residue) and a C-Terminal Flag- tag (8 AA residue).

    Source

    HEK293 cell line.

    Formulation

    Filtered (0.4 µm) and lyophilized in 20 mM Tris buffer, 50 mM NaCl, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adiponectin, also referred to as Acrp30, AdipoQ and GBP-28, is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

    • Synonyms

      Adipocyte C1q and collagen domain-containing protein, Adipocyte complement-related 30kDa protein, Adipose most abundant gene transcript 1 protein, gelatin-binding protein, Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ACRP30 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ACRP30 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

      Add deionized water to a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      GITATEGPGA LVPPPKETCA GWMAGIPGYP GHNGIPGRDG RDGTPGEKGE KGDAGVLGPK GDPGDAGMTG AEGPRGFPGT PGRKGEPGEA AYMYHSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFHCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA SGSMLLHLEV GDQVWLQVYG EGDNNGLYAD NVNDSTFTGF LLYHDTNAAADYKDDDDK

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 25.7kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293 cell line.

      What is the Purity of ADIPONECTIN Protein?
      ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      GITATEGPGA LVPPPKETCA GWMAGIPGYP GHNGIPGRDG RDGTPGEKGE KGDAGVLGPK GDPGDAGMTG AEGPRGFPGT PGRKGEPGEA AYMYHSAFSV GLETRVTVPN VPIRFTKIFY NQQNHYDGST GKFHCNIPGL YYFSYHITVY MKDVKVSLFK KDKAVLFTYD QYQEKNVDQA SGSMLLHLEV GDQVWLQVYG EGDNNGLYAD NVNDSTFTGF LLYHDTNAAADYKDDDDK.

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

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

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

    Acrp30 Rat
  • View Data Sheet

    Name :

    SERPINA3

    Description:

    Alpha-1 AntiChymotrypsin Human Recombinant

    Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    Product # :

    PRO-750

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    Description

    SERPINA3 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 421 amino acids (24-423 a.a.) and having a molecular mass of 47.6 kDa.The SERPINA3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SERPINA3 solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1-ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
      Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT.

    • Synonyms

      Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    • 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 MHPNSPLDEE NLTQENQDRG THVDLGLASA NVDFAFSLYK QLVLKAPDKN VIFSPLSIST ALAFLSLGAH NTTLTEILKG LKFNLTETSE AEIHQSFQHL LRTLNQSSDE LQLSMGNAMF VKEQLSLLDR FTEDAKRLYG SEAFATDFQD SAAAKKLIND YVKNGTRGKI TDLIKDLDSQ TMMVLVNYIF FKAKWEMPFD PQDTHQSRFY LSKKKWVMVP MMSLHHLTIP YFRDEELSCT VVELKYTGNA SALFILPDQD KMEEVEAMLL PETLKRWRDS LEFREIGELY LPKFSISRDY NLNDILLQLG IEEAFTSKAD LSGITGARNL AVSQVVHKAV LDVFEEGTEA SAATAVKITL LSALVETRTI VRFNRPFLMI IVPTDTQNIF FMSKVTNPKQ 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.

    Serpina3 Human Recombinant
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    Name :

    Protein-A/G/L

    Description:

    Protein A/G/L Recombinant

    Product # :

    PRO-1936

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    Description

    Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 805 amino acids in total and having a molecular mass of 89.2kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein- A/G/L was lyophilized without any additives.

    Purity

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

    Citations

    More Info

    • Introduction

      The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NAAQHDEAQQ NAFYQVLNMP NLNADQRNGF IQSLKDDPSQ SANVLGEAQK LNDSQAPKAD AQQNNFNKDQ QSAFYEILNM PNLNEAQRNG FIQSLKDDPS QSTNVLGEAK KLNESQAPKA DNNFNKEQQN AFYEILNMPN LNEEQRNGFI QSLKDDPSQS ANLLSEAKKL NESQAPKADN KFNKEQQNAF YEILHLPNLN EEQRNGFIQS LKDDPSQSAN LLAEAKKLND AQAPKADNKF NKEQQNAFYE ILHLPNLTEE QRNGFIQSLK DDPSVSKEIL AEAKKLNDAQ APKEEDSLEG SGSGTYKLIL NGKTLKGETT TEAVDAATAE KVFKQYANDN GVDGEWTYDD ATKTFTVTEK PEVIDASELT PAVTTYKLVI NGKTLKGETT TKAVDAETAE KAFKQYANDN GVDGVWTYDD ATKTFTVTEE PRARPGSGSG KEETPETPET DSEEEVTIKA NLIFANGSTQ TAEFKGTFEK ATSEAYAYAD TLKKDNGEYT VDVADKGYTL NIKFAGKEKT PEEPKEEVTI KANLIYADGK TQTAEFKGTF EEATAEAYRY ADALKKDNGE YTVDVADKGY TLNIKFAGKE KTPEEPKEEV TIKANLIYAD GKTQTAEFKG TFEEATAEAY RYADLLAKEN GKYTVDVADK GYTLNIKFAG KEKTPEEPKE EVTIKANLIY ADGKTQTAEF KGTFAEATAE AYRYADLLAK ENGKYTADLE DGGYTINIRF AGKKVDEKPE EKEQVTIKEN IYFEDGTVQT ATFKGTFAEA TAEAYRYADL LSKEHGKYTA DLEDGGYTIN IRFAG.

    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.

    Protein A G L
  • View Data Sheet

    Name :

    ANXA1 Human

    Description:

    Annexin A1 Human Recombinant

    ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.

    Product # :

    PRO-679

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    Description

    ANXA1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 346 amino acids (1-346 a.a.) and having a molecular mass of 38.7 kDa.ANXA1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA1 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ANXA1 is part of the family of Ca(2+)-dependent phospholipid binding proteins which have a Mw between 35kDa-40kDa and are situated on the cytosolic face of the plasma membrane. ANXA1 protein has a Mw of 40kDa, with phospholipase A2 inhibitory activity to bind from two to four calcium ions with high affinity. Since phospholipase A2 is necessary for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, ANXA1 might have potential anti-inflammatory activity. ANXA1 promotes membrane fusion and iplays a role in exocytosis. The recognition of ANXA1 protein by immunocytochemical leads a simple, highly sensitive and specific assay for diagnosis of hairy cell leukemia.

    • Synonyms

      ANX1, LPC1, ANXA1, Lipocortin I, Calpactin II, Chrombindin-9, p35, Annexin-1, Phospholipase A2 inhibitory protein, Annexin I, Annexin A1.

    • 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

      MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV DEATIIDILT KRNNAQRQQI KAAYLQETGK
      PLDETLKKAL TGHLEEVVLA LLKTPAQFDA DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL
      LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY TKYSKHDMNK VLDLELKGDI EKCLTAIVKCATSKPAFFAE KLHQAMKGVG TRHKALIRIM VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN.

    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.

    Anxa1 Human
  • View Data Sheet

    Name :

    PCSK1N Human

    Description:

    Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor Human Recombinant

    ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    Product # :

    PRO-1819

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    Description

    PCSK1N Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (34-260) and having a molecular mass of 26.6 kDa.PCSK1N is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PCSK1N solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.

    • Synonyms

      ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    • 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 MGSMARPVKE PRGLSAASPP LAETGAPRRF RRSVPRGEAA GAVQELARAL AHLLEAERQE RARAEAQEAE DQQARVLAQL LRVWGAPRNS DPALGLDDDP DAPAAQLARA LLRARLDPAA LAAQLVPAPV PAAALRPRPP VYDDGPAGPD AEEAGDETPD VDPELLRYLL GRILAGSADS EGVAAPRRLR RAADHDVGSE LPPEGVLGAL LRVKRLETPA PQVPARRLLP P.

    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.

    Pcsk1N Human
  • View Data Sheet

    Name :

    Aln G 1.0101

    Description:

    Major pollen allergen Aln g 1 Recombinant

    Major pollen allergen Aln g 1, Allergen Aln g I, Aln g 1.

    Product # :

    PRO-2280

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    Description

    Recombinant Major pollen allergen Aln g 1 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 18,710 Dalton. Aln G 1.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Aln G 1.0101 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Major pollen allergen Aln g 1 (Aln G 1.0101) causes an allergic reaction in humans.

    • Synonyms

      Major pollen allergen Aln g 1, Allergen Aln g I, Aln g 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

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

    • Molar extinction coefficient

      7450; A280(1mg/ml)=0.398

    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.

    Aln G 10101
  • View Data Sheet

    Name :

    Thrombin

    Description:

    Human Thrombin

    Product # :

    PRO-339

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    Description

    Thrombin was purified from human plasma.

    Source

    Human Plasma.

    Formulation

    Lyophilized protein containing mannitol, sodium chloride, calcium chloride.

    Biological Activity

    The specific activity was found to be 116 US Units/mg protein.

    Citations

    More Info

    • Introduction

      Thrombin enzyme (Activated Factor IIa) is an important clotting promoter that controls the transformation of soluble fibrinogen to insoluble active fibrin strands. Thrombin is a coagulation protein and a serine protease (EC 3.4.21.5) that catalyzes many coagulation-related reactions. Thrombin triggers factor-XI, factor-V, Factor-XIII and factor-VIII. Thrombin endorses platelet activation, using activation of protease-activated receptors on the platelet. As a result of its high proteolytic specificity, thrombin has become an important biochemical protein. The thrombin cleavage site (Leu-Val-Pro-Arg-Gly-Ser) is widely used in linker regions of recombinant fusion protein constructs. After the purification of the fusion protein, thrombin is used to cleave between the Arginine and Glycine residues of the cleavage site, efficiently removing the purification tag from the protein of interest with a high degree of specificity.

    • Physical Appearance

      lyophilized powder.

    • Stability

      Lyophilized Human Thrombin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution human thrombin 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 human thrombin in sterile a 0.9% NaCl solution at 500U/ml.

    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.

    Thrombin Human
  • View Data Sheet

    Name :

    Omentin 298 a.a. Human

    Description:

    Omentin 298 a.a. Human Recombinant

    Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    Product # :

    CYT-061

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    Description

    Omentin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (17-313) and having a molecular mass of 33.2 kDa.The Omentin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Omentin protein (1mg/ml) is supplied in 20mM Tris-HCL, pH-8, 0.4M Urea and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

    • Synonyms

      Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    • 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

      MWSTDEANTY FKEWTCSSSP SLPRSCKEIK DECPSAFDGL YFLRTENGVI YQTFCDMTSG GGGWTLVASV HENDMRGKCT VGDRWSSQQG SKAVYPEGDG NWANYNTFGS AEAATSDDYK NPGYYDIQAK DLGIWHVPNK SPMQHWRNSS LLRYRTDTGF LQTLGHNLFG IYQKYPVKYG EGKCWTDNGP VIPVVYDFGD AQKTASYYSP YGQREFTAGF VQFRVFNNER AANALCAGMR VTGCNTEHHC IGGGGYFPEA SPQQCGDFSG FDWSGYGTHV GYSSSREITE AAVLLFYR

    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.

    Omentin 298 Aa Human
  • View Data Sheet

    Name :

    FURIN Human

    Description:

    Furin Human Recombinant

    Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

    Product # :

    PRO-2199

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    Description

    FURIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids (108-715 a.a) and having a molecular mass of 69.8kDa. FURIN is fused to a 37 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Furin is a member of the peptidase S8 family. Furin signifies the ubiquitous endoprotease activity within constitutive secretory pathwaysas well as capable of cleavage at the RX (K/R) R consensus motif.Furin is considered to be one of the proteases responsible for the activation of HIV envelope glycoproteins gp160 as well as gp140 and might take part in tumor progression. Among the diseases associated with FURIN are dementia, familial british and plague.

    • Synonyms

      Furin (Paired Basic Amino Acid Cleaving Enzyme), PCSK3, PACE, FUR, Paired Basic Amino Acid Residue-Cleaving Enzyme, EC 3.4.21.75, Paired Basic Amino Acid Cleaving Enzyme (Furin, Membrane Associated Receptor Protein), Proprotein Convertase Subtilisin/Kexin Type 3, Furin, Membrane Associated Receptor Protein, Dibasic Processing Enzyme, Dibasic-Processing Enzyme, FES Upstream Region, EC 3.4.21, Furin, SPC1, Dibasic-processing enzyme, Paired basic amino acid residue-cleaving enzyme.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMDVY QEPTDPKFPQ QWYLSGVTQR DLNVKAAWAQ GYTGHGIVVS ILDDGIEKNH PDLAGNYDPG ASFDVNDQDP DPQPRYTQMN DNRHGTRCAG EVAAVANNGV CGVGVAYNAR IGGVRMLDGE VTDAVEARSL GLNPNHIHIY SASWGPEDDG KTVDGPARLA EEAFFRGVSQ GRGGLGSIFV WASGNGGREH DSCNCDGYTN SIYTLSISSA TQFGNVPWYS EACSSTLATT YSSGNQNEKQ IVTTDLRQKC TESHTGTSAS APLAAGIIAL TLEANKNLTW RDMQHLVVQT SKPAHLNAND WATNGVGRKV SHSYGYGLLD AGAMVALAQN WTTVAPQRKC IIDILTEPKD IGKRLEVRKT VTACLGEPNH ITRLEHAQAR LTLSYNRRGD LAIHLVSPMG TRSTLLAARP HDYSADGFND WAFMTTHSWD EDPSGEWVLE IENTSEANNY GTLTKFTLVL YGTAPEGLPV PPESSGCKTL TSSQACVVCE EGFSLHQKSC VQHCPPGFAP QVLDTHYSTE NDVETIRASV CAPCHASCAT CQGPALTDCL SCPSHASLDP VEQTCSRQSQ SSRESPPQQQ PPRLPPEVEA GQRLRAGLLP SHLPE.

    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.

    Furin Human
  • View Data Sheet

    Name :

    Cys-Protein-A/G/L

    Description:

    Cys-Protein A/G/L Recombinant

    Product # :

    PRO-1935

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    Description

    Recombinant Protein-A/G/L produced in E.Coli is a single non-glycosylated polypeptide chain fused with a Cys at N-terminus. Protein- A/G/L is comprised of 5 IgG-binding regions of Protein A (E-D-A-B-C), 2 of protein G (C1-C3) and 5 of Protein L (B1-B2-B3-B4-B5) containing 806 amino acids in total and having a molecular mass of 89.3kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein- A/G/L to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein- A/G/L was lyophilized without any additives.

    Purity

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

    Citations

    More Info

    • Introduction

      The recombinant Protein A/G/L is a genetically engineered protein which combines the IgG binding profiles of all Protein A, Protein G and Protein L. Protein A/G/L is a gene fusion product. Recombinant fusion protein A/G/L is comprised of 5 Ig-binding regions of protein L (B1-B2-B3-B4-B5), 5 IgG binding domains from Protein A (E-D-A-B-C) and 2 Ig-binding region of protein G (C1-C3). The recombinant Protein A/G/L is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G/L binds to IgG from humans, mice, rats, cows, goats, sheep, rabbits, guinea pigs, pigs, dogs and cats.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Protein-A/G/L although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein-A/G/L 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 Protein-A/G/L in sterile 18M-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE GSGSGTYKLI LNGKTLKGET TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE EPRARPGSGS GKEETPETPE TDSEEEVTIK ANLIFANGST QTAEFKGTFE KATSEAYAYA DTLKKDNGEY TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT FEEATAEAYR YADALKKDNG EYTVDVADKG YTLNIKFAGK EKTPEEPKEE VTIKANLIYA DGKTQTAEFK GTFEEATAEA YRYADLLAKE NGKYTVDVAD KGYTLNIKFA GKEKTPEEPK EEVTIKANLI YADGKTQTAE FKGTFAEATA EAYRYADLLA KENGKYTADL EDGGYTINIR FAGKKVDEKP EEKEQVTIKE NIYFEDGTVQ TATFKGTFAE ATAEAYRYAD LLSKEHGKYT ADLEDGGYTI NIRFAG.

    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.

    Cys Protein A G L
  • View Data Sheet

    Name :

    CALB2 Human

    Description:

    Calbindin-2 Human Recombinant

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

    Product # :

    PRO-401

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Calb2 Human
  • View Data Sheet

    Name :

    ATF Bovine

    Description:

    Apo Transferrin Bovine

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

    Product # :

    PRO-511

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    Description

    Bovine Apo Transferrin is a glycoprotein of approximately 77kDa.

    Source

    Bovine Serum.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

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

    • Stability

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

    • Solubility

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

    • Iron Content

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

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

    Apo Transferrin Bovine
  • View Data Sheet

    Name :

    HBsAg adw

    Description:

    Hepatitis B Surface Antigen, adw Recombinant

    Product # :

    HBS-872

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    Description

    HbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.

    Source

    Pichia Pastoris.

    Formulation

    Sterile Filtered solution containing 20mM Phosphate Buffer, 154mM sodium chloride, pH 7.1.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.

    • Physical Appearance

      Sterile Filtered pale solution.

    • Stability

      HBsAg Should be stored at 4°C.DO NOT FREEZE.

    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.

    Hbsag Adw
  • View Data Sheet

    Name :

    Adiponectin Mouse, Trimeric

    Description:

    Adiponectin Mouse Recombinant, Trimeric form

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-247

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    Description

    Trimeric form of Acrp30 Mouse was expressed in HEK293 cells.The cysteine 39 was replaced with alanine (C39A) 9. mAd-C39A can only form trimer, but not hexamer or HMW form.

    Source

    HEK293 (Human embryonic kidney cell line).

    Formulation

    Mouse Acrp30 filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M phosphate buffer, 0.05M NaCl, pH 7.2.

    Purity

    Acrp30 Mouse purity is greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Adiponectin is a hormone exclusively expressed from adipose tissue. Many studies demonstrate that adiponectin has direct anti-diabetic, anti-atherogenic and anti-inflammatory functions. APM-1 can increase insulin sensitivity of skeletal muscle, attenuate hepatic lipogenesis and luconeogenesis, regulate NO production in endothelial cells, inhibit proliferation of smooth muscle cells and prevent lipid accumulation of macrophage cells.
      In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (MMW, also called trimer) forms 8. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • Physical Appearance

      Filtered white lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Acrp30 Mouse at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Mouse can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 26kDa.

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293

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

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

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

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

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

    Adiponectin Mouse Trimeric
  • View Data Sheet

    Name :

    Leptin Protein

    Description:

    Leptin Human Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-228

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

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

    Description

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological Activity is evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

    Citations

    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 Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Leptin in sterile water or 0.4% NaHCO3 pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.87 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

    Leptin Human
  • View Data Sheet

    Name :

    Inhibin a Human

    Description:

    Inhibin Alpha Human Recombinant

    Product # :

    HOR-303

    Price :

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    Shipped with Ice Packs

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

    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.

    Citations

    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 :

    Cor a 1.0103

    Description:

    Major pollen allergen Cor a 1 Recombinant

    Major pollen allergen Cor a 1 isoforms 5, 6, 11 and 16, Allergen Cor a I, Cor a 1, Cor a 1.0103.

    Product # :

    PRO-2285

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

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

    Description

    Recombinant Major pollen allergen Cor a 1 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 17,470 Dalton. Cor a 1.0103 purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Cor a 1.0103 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Major pollen allergen Cor a 1 (Cor a 1.0103) causes an allergic reaction in human. The Cor a 1 isoforms exhibit different antigenic and allergenic properties.

    • Synonyms

      Major pollen allergen Cor a 1 isoforms 5, 6, 11 and 16, Allergen Cor a I, Cor a 1, Cor a 1.0103.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

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

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

    Cor A 10103
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