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Search results

1000 results found for “parvalbumin”

Name

Description

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  • View Data Sheet

    Name :

    Streptavidin-NC

    Description:

    Streptavidin-NC Recombinant

    Product # :

    PRO-338

    Price :

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    Description

    Recombinant Streptavidin-NC produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 24kDa. Streptavidin-NC is engineered to bind to nitrocellulose.

    Source

    Escherichia Coli.

    Formulation

    The sterile solution contains 10mM K2HPO4-KH2PO4, pH 7.3.

    Purity

    Greater than 93.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Streptavidin is a tetrameric protein secreted by Streptomyces avidinii which binds firmly to biotin. Streptavidin is wilyde used in molecular biology through its unique high affinity for the vitamin biotin. The dissociation constant (Kd) of the biotin-streptavidin complex is about ~10-15 mol/L. The strong affinity recognition of biotin and biotinylated molecules has made streptavidin one of the most important components in diagnostics and laboratory kits. The streptavidin/biotin system has one of the biggest free energies of association of yet observed for noncovalent binding of a protein and small ligand in aqueous solution (K_assoc = 10**14). The complexes are also extremely stable over a wide range of temperature and pH.

    • Physical Appearance

      Sterile Liquid formulation.

    • Stability

      Streptavidin-NC although stable at 4°C for 3 weeks, should be stored below -18°C. Please prevent 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.

    Streptavidin Nc
  • View Data Sheet

    Name :

    AREG Human

    Description:

    Amphiregulin Human Recombinant

    Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.

    Product # :

    CYT-041

    Price :

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    • More Info

    Description

    Amphiregulin (AREG) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.3 KDa.The AREG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.4.

    Purity

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

    Biological Activity

    Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

    More Info

    • Synonyms

      Schwannoma-derived growth factor, Colorectum cell-derived growth factor, AR, CRDGF, SDGF, AREGB, MGC13647.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.

    • Background

      Amphiregulin Human Recombinant: Exploring its Role in Cancer Biology and Therapeutic Applications

      Abstract:


      Amphiregulin, a member of the epidermal growth factor (EGF) family, has gained significant attention in cancer research. This research paper provides an overview of Amphiregulin human recombinant, highlighting its molecular characteristics, signaling pathways, and therapeutic potential. Understanding the multifaceted role of Amphiregulin opens avenues for targeted cancer therapies. This article provides a concise analysis of Amphiregulin, emphasizing its impact on cancer biology and its therapeutic applications.

      Introduction:


      Cancer continues to be a significant health challenge worldwide, necessitating novel therapeutic approaches. Amphiregulin, an EGF family member, has emerged as a promising target in cancer research. This paper provides an overview of Amphiregulin, shedding light on its structure, function, and therapeutic potential.

      Amphiregulin Signaling and Mechanisms:


      Amphiregulin exerts its effects through the binding and activation of the EGF receptor (EGFR). Upon activation, a cascade of intracellular signaling pathways is triggered, including the MAPK and PI3K/AKT pathways. These pathways regulate critical cellular processes such as cell proliferation, survival, migration, and angiogenesis.

      Amphiregulin in Cancer Biology:


      Amphiregulin has been implicated in various aspects of cancer biology, including tumor growth, metastasis, and resistance to therapy. Its overexpression is observed in several cancer types, and its role in promoting tumor growth and metastasis has been demonstrated in preclinical studies. Targeting Amphiregulin signaling shows promise in inhibiting cancer progression and overcoming therapy resistance.

      Therapeutic Potential of Amphiregulin Human Recombinant:


      Amphiregulin human recombinant holds significant therapeutic potential in cancer treatment. Strategies aimed at blocking Amphiregulin-EGFR interactions or inhibiting downstream signaling pathways are being explored as potential therapeutic interventions. Additionally, Amphiregulin could serve as a predictive biomarker to identify patients who are more likely to respond to targeted therapies.

      Challenges and Future Directions:


      While the therapeutic targeting of Amphiregulin shows promise, several challenges need to be addressed. Further research is required to fully understand the complex interplay between Amphiregulin and other molecular pathways in cancer biology. Additionally, the development of specific and potent inhibitors and the identification of patient selection criteria are important considerations for successful clinical translation.

      Conclusion:


      Amphiregulin human recombinant represents a promising avenue for targeted cancer therapy. Understanding the molecular mechanisms and functional implications of Amphiregulin in cancer biology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve patient outcomes and contribute to the advancement of personalized medicine.

      What is the molecular weight/Mw of AREG Protein?
      AREG Protein has a total Mw of 11.3kDa.

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

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

      What is the Biological Activity of AREG Protein?
      Determined by its ability to stimulate the proliferation of mouse Balb/c 3T3 cells. The expected ED50 for this effect is 5-10 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

      What is the amino acid sequence of AREG Protein?
      SVRVEQVVKP PQNKTESENT SDKPKRKKKG GKNGKNRRNR KKKNPCNAEF QNFCIHGECK YIEHLEAVTC KCQQEYFGER CGEKSMKTHS MIDSSLSK.

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

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

    Areg Human
  • View Data Sheet

    Name :

    HCV NS5

    Description:

    Hepatitis C Virus NS5 Recombinant

    Product # :

    HCV-235

    Price :

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    Description

    The E.coli derived recombinant protein contains the HCV NS5a immunodominant regions, amino acids 2061-2302. The protein is fused with GST at N-terminus.

    Formulation

    1.5M Urea, 25mM Tris-HCl pH 8, 50% glycerol and 0.2% Triton-X.

    Purity

    HCV-NS5 protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
      HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).

    • Stability

      HCV NS5 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      HCV-NS5 antigen is suitable for ELISA and Western blots, excellent antigen for detection of HCV with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of HCV-infected individuals.

    • Purification Method

      HCV-NS5 protein was purified by proprietary 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.

    Hcv Ns5
  • View Data Sheet

    Name :

    AGA Human, sf9

    Description:

    Aspartylglucosaminidase Human Recombinant, sf9

    Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.

    Product # :

    ENZ-990

    Price :

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    Description

    AGA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 332 amino acids (24-346 a.a.) and having a molecular mass of 35.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-57kDa). AGA is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    AGA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aspartylglucosaminidase, also known as AGA, takes part in the catabolism of Nlinked oligosaccharides of glycoproteins. AGA is a protein coding gene which cleaves asparagine from N-acetylglucosamines in the lysosomal breakdown of glycoproteins.

    • Synonyms

      Aspartylglucosaminidase, Glycosylasparaginase, N4-(N-Acetyl-Beta-Glucosaminyl)-L-Asparagine Amidase, N(4)-(Beta-N-Acetylglucosaminyl)-L-Asparaginase , EC 3.5.1.26, Aspartylglucosylamine Deaspartylase, EC 3.5.1, ASRG, AGU, GA.

    • 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

      ADPSSPLPLV VNTWPFKNAT EAAWRALASG GSALDAVESG CAMCEREQCD GSVGFGGSPD ELGETTLDAM IMDGTTMDVG AVGDLRRIKN AIGVARKVLE HTTHTLLVGE SATTFAQSMG FINEDLSTTA SQALHSDWLA RNCQPNYWRN VIPDPSKYCG PYKPPGILKQ DIPIHKETED DRGHDTIGMV VIHKTGHIAA GTSTNGIKFK IHGRVGDSPI PGAGAYADDT AGAAAATGNG DILMRFLPSY QAVEYMRRGE DPTIACQKVI SRIQKHFPEF FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCIHHHH HH.

    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.

    Aga Human Sf9
  • View Data Sheet

    Name :

    ANXA2 Human

    Description:

    Annexin A2 Human

    ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.

    Product # :

    PRO-1573

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    Description

    The Human Annexin A2 produced from Human Adipose Tissue has a molecular mass of 38.472kDa (calculated without glycosylation) containing 338 amino acid residues.

    Source

    Human Adipose Tissue.

    Formulation

    ANXA2 protein filtered (0.4µm) and lyophilized in 0.5mg/ml in 0.05M phosphate buffer, 0.075M NaCl and pH 6.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ANXA2 is part of the annexin family and is involved in the regulation of cellular growth and in signal transduction pathways. ANXA2 protein functions as an autocrine factor which increases osteoclast formation and bone resorption. ANXA2 is associated with sickle cell osteonecrosis. Reduced ANXA2 expression is associated with osteosarcoma metastases. ANXA2 is part of the putative cell surface vitamin D binding protein binding site complex and functions to mediate the chemotactic cofactor effect. ANXA2 is involved in dysferlin deficiency and in muscular dystrophies. Human colon adenocarcinoma cell differentiation is related with an up-regulation of ANXA2.

    • Synonyms

      ANX2, ANX2L4, CAL1H, LIP2, LPC2, LPC2D, P36, PAP-IV, ANXA2, Annexin A2, Annexin-2, Annexin II, Lipocortin II, Calpactin-1 heavy chain, Calpactin I heavy chain, Chromobindin-8, p36, Protein I, Placental anticoagulant protein IV.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      STVHEILCKL SLEGDHSTPP SAYGSVKAYT NFDAERDALN IETAIKTKGV DEVTIVNILT NRSNAQRQDI AFAYQRRTKK ELASALKSAL SGHLETVILG LLKTPAQYDA SELKASMKGL GTDEDSLIEI ICSRTNQELQ EINRVYKEMY KTDLEKDIIS DTSGDFRKLM VALAKGRRAE DGSVIDYELI DQDARDLYDA GVKRKGTDVP KWISIMTERS VPHLQKVFDR YKSYSPYDML ESIRKEVKGD LENAFLNLVQ CIQNKPLYFA DRLYDSMKGK GTRDKVLIRI MVSRSEVDML KIRSEFKRKY GKSLYYYIQQ DTKGDYQKAL LYLCGGDD.

    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.

    Human Anxa2
  • 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 :

    MBL2 Human, Sf9

    Description:

    Mannose-Binding Lectin 2 Human Recombinant, Sf9

    Mannose Binding Lectin 2, Mannose-Binding Lectin (Protein C) 2, Soluble (Opsonic Defect), Collectin-1, COLEC1, MBP-C, MBP1, MBL, Mannose-Binding Lectin 2, Soluble (Opsonic Defect), Mannose-Binding Lectin (Protein C) 2, Soluble, Mannose-Binding Protein C, Mannan-Binding Protein, Mannose-Binding Lectin, Mannan-Binding Lectin, HSMBPC, MBL2D, MBPD, MBP.                

    Product # :

    PRO-2526

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    Description

    MBL2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 237 amino acids (21-248a.a.) and having a molecular mass of 25.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). MBL2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MBL2 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mannose-binding protein C (MBL2), belongs to the collectin family of patternrecognition molecules and is an important component in the innate immune system. MBL2 is a secreted glycoprotein which recognizes mannose and N-acetylglucosamine on various microorganisms, and is capable of activating the classical complement pathway. Lacking MBL2 has been associated with susceptibility to autoimmune and infectious diseases.

    • Synonyms

      Mannose Binding Lectin 2, Mannose-Binding Lectin (Protein C) 2, Soluble (Opsonic Defect), Collectin-1, COLEC1, MBP-C, MBP1, MBL, Mannose-Binding Lectin 2, Soluble (Opsonic Defect), Mannose-Binding Lectin (Protein C) 2, Soluble, Mannose-Binding Protein C, Mannan-Binding Protein, Mannose-Binding Lectin, Mannan-Binding Lectin, HSMBPC, MBL2D, MBPD, MBP.

    • 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

      ADPETVTCED AQKTCPAVIA CSSPGINGFP GKDGRDGTKG EKGEPGQGLR GLQGPPGKLG PPGNPGPSGS PGPKGQKGDP GKSPDGDSSL AASERKALQT EMARIKKWLT FSLGKQVGNK FFLTNGEIMT FEKVKALCVK FQASVATPRN AAENGAIQNL IKEEAFLGIT DEKTEGQFVD LTGNRLTYTN WNEGEPNNAG SDEDCVLLLK NGQWNDVPCS TSHLAVCEFP IHHHHHH

    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.

    Mbl2 Protein
  • View Data Sheet

    Name :

    VPS29 Human

    Description:

    Vacuolar Protein Sorting 29 Human Recombinant

    Vacuolar protein sorting 29 yeast homolog (S. cerevisiae), DC15, PEP11, DC7, retromer protein, x 007 protein, EC 3.1.3.3.

    Product # :

    PRO-1075

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    Description

    VPS29 Human Recombinant produced in E. coli is a single polypeptide chain containing 207 amino acids (1-182) and having a molecular mass of 23.2kDa.VPS29 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The VPS29 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      VPS29 is a member of a group of genes coding for vacuolar protein sorting (VPS) proteins which, when functionally damaged, lessens the efficient transfer of vacuolar hydrolases. VPS29 is a late Golgi transmembrane protein that operates as the sorting receptor for soluble vacuolar hydrolases, from the prevacuolar endosome back to the Golgi. Moreover, VPS29 takes part in the creation of the inner shell of the retromer coat for retrograde vesicles parting the prevacuolar compartment.

    • Synonyms

      Vacuolar protein sorting 29 yeast homolog (S. cerevisiae), DC15, PEP11, DC7, retromer protein, x 007 protein, EC 3.1.3.3.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSHMMLVLV LGDLHIPHRC NSLPAKFKKL LVPGKIQHIL CTGNLCTKES YDYLKTLAGD VHIVRGDFDE NLNYPEQKVV TVGQFKIGLI HGHQVIPWGD MASLALLQRQ FDVDILISGH THKFEAFEHE NKFYINPGSA TGAYNALETN IIPSFVLMDI QASTVVTYVY QLIGDDVKVE RIEYKKP

    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.

    Vps29 Human
  • View Data Sheet

    Name :

    ACE2 (18-740) Human, Biotin

    Description:

    Angiotensin Converting Enzyme 2 (18-740 a.a.), Biotinylated Human Recombinant

    Product # :

    ENZ-1127

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    Description

    The HEK293 derived ACE2 Human recombinant biotinylated protein contains the amino acids Gln 18-Ser 740 fused to His-AVI tag at C-terminal having a predicted Mw of 87.2 kDa ( migrates 95-125 kDa under reducing conditions on sds-page due to glycosilation). ACE2 Protein binds to SARS Coronavirus-2 [ CoV-2019 ] Spike receptor binding domain.

    Source

    HEK293 Cells

    Formulation

    ACE2 Human protein solution is supplied in 50mM Tris, pH7.5, 150mM NaCl and 20% glycerol.

    Purity

    ACE-2 Protein is >90% pure as determined SDS-PAGE.

    Biological Activity

    ACE2 activity was measured by its binding ability in a functional ELISA.

    The immobilized Recombinant Human ACE2 protein binds to SARS CoV2 Spike protein Receptor Binding Domain at 2ug per ml.

    More Info

    • Introduction

      ACE-2 (Angiotensin converting enzyme 2) an enzyme bound to cell membranes in various organs such as intestines arteries , lungs, heart & kidney. ACE2 an entry receptor of SARS coronaviruses as well as SARS-CoV-2,.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen located on the external envelope of the virion that takes part in a critical part in viral infection by identifying host cell receptors and facilitating fusion of the viral and cellular membranes. 2 main domains in coronavirus S1 have been recognized, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains function as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 obtains a signal peptide, a transmembrane domain, and a single metalloproteinase active site containing an HEXXH zinc-binding domain. ACE-2 plays a role as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      ACE-2 Human Recombinant Protein is shipped on ice packs. Upon arrival, Store at -20°C. The addition of 0.1% albmin is highly recommended for long term storage use.

    • Purification Method

      Purified by Protein-G 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.

    Ace 2 Protein
  • View Data Sheet

    Name :

    Protein-A/G, His

    Description:

    Protein A/G Recombinant, His Tag

    Product # :

    PRO-1927

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    Description

    Protein-A/G Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain fused with a 6×His tag at C-terminus. Protein-A/G is comprised of 5 IgG-binding regions of protein A (E-D-A-B-C) and 3 of protein G (C1-C2-C3) containing 513 amino acids in total and having a molecular mass of 56.9kDa. Cell wall binding region, cell membrane binding region and albumin binding region have been eliminated from the recombinant Protein A/G to guarantee the maximum specific IgG binding.

    Source

    Escherichia Coli.

    Formulation

    Protein-A/G was lyophilized without any additives.

    Purity

    Greater than 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      The recombinant Protein A/G is a genetically engineered protein comprised of 8 IgG-binding domains EDABC-C1C2C3, corresponding to the Protein A and G domains which are included in the recombinant sequence. The Protein A part is from Staphylococcus aureus segments E, D, A, B and C. The Protein G part is from Streptococcus segments C1, C2 and C3. The recombinant Protein A/G has a broader binding capacity than either Protein A or Protein G alone. The recombinant Protein A/G is ideal for purification of monoclonal or polyclonal IgG antibodies. Protein A/G binds to various human, mouse and rat IgG subclasses such as the human IgG1, IgG2, IgG3, IgG4; mouse IgG2a, IgG2b, IgG3 and rat IgG2a, IgG2c. In addition, Protein A/G binds to total IgG from cow, goat, sheep, horse, rabbit, guinea pig, pig, dog and cat.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MNAAQHDEAQ 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 TTEAVDAATA EKVFKQYAND NGVDGEWTYD DATKTFTVTE KPEVIDASEL TPAVTTYKLV INGKTLKGET TTKAVDAETA EKAFKQYAND NGVDGVWTYD DATKTFTVTE KLAAALEHHH 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.

    Protein A G His
  • View Data Sheet

    Name :

    Leptin Human, His

    Description:

    Leptin Human Recombinant, His Tag

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-287

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    Description

    Leptin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing amino acids 48-167 and having a total molecular mass of 19 kDa including the 4 kDa His tag.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Leptin is a protein hormone with important effects in regulating body weight, metabolism and reproductive function. The protein is approximately~16 kDa in mass and encoded by the obese (ob)gene. leptin is expressed predominantly by adipocytes, which fits with the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus known to be important in regulating body weight, as well as in T lymphocytes and vascular endothelial cells.

    • 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, should be stored desiccated below 0°C. Reconstituted Leptin is best stored refrigerated at 4°C.Please avoid freeze-thaw cycles.

    • Solubility

      The lyophilized Leptin is very soluble in water and most aqueous buffers below and above the isoelectric point.

    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 His
  • View Data Sheet

    Name :

    CXCL8 Human (1-77)

    Description:

    Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8)

    IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    Product # :

    CHM-327

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    • sds-page

    Description

    Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8904 Dalton. The IL-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.

    sds-page

    IL8 Human sds-page - Product image 1

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 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 Interleukin 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.

    • Background

      What is the molecular weight/Mw of CXCL8 HUMAN (1-77) Protein?
      CXCL8 HUMAN (1-77) Protein has a total Mw of 8.9kDa.

      What is the source or expression system of CXCL8 HUMAN (1-77) Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 HUMAN (1-77) Protein?
      CXCL8 HUMAN (1-77) Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN (1-77) Protein?
      Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.

      What is the amino acid sequence of CXCL8 HUMAN (1-77) Protein?
      AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.

      What applications can CXCL8 HUMAN (1-77) Protein be used in?
      CXCL8 HUMAN (1-77) Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 HUMAN (1-77) Protein?
      The endotoxin level is minimal, CXCL8 HUMAN (1-77) 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.

    Il 8 77 Human
  • View Data Sheet

    Name :

    GDNF Human, Sf9

    Description:

    Glial-Derived Neurotrophic Factor Human Recombinant, Sf9

    Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.

    Product # :

    CYT-1162

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    • More Info

    Description

    GDNF Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 113amino acids (109-211 aa) and having a molecular mass of 12.8kDa.GDNF is fused to an 10 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GDNF protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glial cell-derived neurotrophic factor or GDNF is part of the GDNF group of ligands proteins. GDNF has a crucial part in numerous cell mechanisms such as neurite outgrowth, cell differentiation, cell survival and migration of cells. GDNF enhances neurons survival via GFRa receptors (mainly GFRa1). The mentioned neurons can die as a result from Parkinson's disease or ALS (amyotrophic lateral sclerosis). This protein takes part in the development of the spermatogenesis & kidney, also, it has a role in alcohol metabolism as ameliorating.

    • Synonyms

      Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, ATF1, ATF2, HFB1-GDNF, HSCR3.

    • 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

      ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH

    • Background

      What is the molecular weight/Mw of GDNF HUMAN, SF9 Protein?
      GDNF HUMAN, SF9 Protein has a total Mw of 12.8kDa.

      What is the source or expression system of GDNF HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of GDNF HUMAN, SF9 Protein?
      GDNF HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDNF HUMAN, SF9 Protein?
      The biological functionality of GDNF HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of GDNF HUMAN, SF9 Protein?
      ADPMRGQRGK NRGCVLTAIH LNVTDLGLGY ETKEELIFRY CSGSCDAAET TYDKILKNLS RNRRLVSDKV GQACCRPIAF DDDLSFLDDN LVYHILRKHS AKRCGCIHHH HHH

      What applications can GDNF HUMAN, SF9 Protein be used in?
      GDNF HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDNF HUMAN, SF9 Protein?
      The endotoxin level is minimal, GDNF HUMAN, SF9 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.

    Gdnf Protein
  • View Data Sheet

    Name :

    Pramlintide

    Description:

    Pramlintide

    Product # :

    HOR-300

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    Description

    Pramlintide Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 3949.4 Dalton and a Molecular formula of C171H267N51O53S2.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Pramlintide acetate is a hormone that is released into the bloodstream, in a similar pattern as insulin. Pramlintide aids in the absorption of glucose by slowing gastric emptying, promoting satiety, and inhibiting inappropriate secretion of glucagon, a catabolic hormone that opposes the effects of insulin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pramlintide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Pramlintide 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 Pramlintide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions. The Pramlintide is also soluble in 1% Acetic Acid.

    • Amino Acid Sequence

      KCNTATCATNRLANFLVHSSNNFGPILPPTNVGSNTY-NH2.

    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.

    Pramlintide
  • View Data Sheet

    Name :

    Thyroglobulin Human

    Description:

    Thyroglobulin Human Recombinant

    Thyroglobulin, TGN, AITD3, TG.

    Product # :

    PRO-2803

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    • sds-page

    Description

    Thyroglobulin Human produced in a mammalian cell line is a single, non-glycosylated polypeptide chain (1-2768 a.a.) and having a molecular mass of 304640 Dalton. Thyroglobulin Human is fused with GlyAlaProGly4SerHis10-tag at C-terminal and purified by proprietary chromatographic techniques.

    Source

    Mammalian cell line.

    Formulation

    Thyroglobulin was lyophilized from PBS, pH 7.4 and 5.4 % sucrose.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    Thyroglobulin Recombinant Human SDS-PAGE - Product image 1

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    • Synonyms

      Thyroglobulin, TGN, AITD3, TG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      Thyroglobulin, a glycoprotein primarily produced in the thyroid gland, stands at the center of thyroid hormone synthesis. Comprising a series of tyrosine residues, thyroglobulin serves as the scaffold upon which thyroid hormones are assembled. Beyond its pivotal role in thyroid physiology, thyroglobulin has garnered significant attention in the realm of thyroid disease diagnostics, offering valuable insights into thyroid function and disorders. This research delves into the intricacies of thyroglobulin human recombinant protein, exploring its biochemical properties, physiological significance, and its crucial applications in both clinical and research settings.

      Structural Complexity of Thyroglobulin:

      Thyroglobulin is a large, dimeric protein boasting an intricate structure composed of multiple domains. Within its structure lie tyrosine residues crucial for iodine incorporation, a process fundamental for thyroid hormone synthesis. Its size and complexity reflect the sophistication of thyroid hormone production, as thyroglobulin acts as a reservoir for thyroid hormones within the thyroid follicles.

      Physiological Significance in Thyroid Function:

      Thyroglobulin plays a central role in the synthesis of triiodothyronine (T3) and thyroxine (T4), the thyroid hormones essential for regulating metabolism and overall body homeostasis. During thyroid hormone synthesis, thyroglobulin is secreted into the follicular lumen, where it undergoes iodination and subsequent proteolysis, releasing T3 and T4. This process highlights the indispensable nature of thyroglobulin in thyroid hormone production, making it a key biomolecule in thyroid physiology.

    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.

    Thyroglobulin Antigen
  • View Data Sheet

    Name :

    XPA Antibody

    Description:

    Xeroderma Pigmentosum Complementation Group A, Mouse Anti Human

    XP1, XPAC, DNA repair protein complementing XP-A cells.

    Product # :

    ANT-504

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    Formulation

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

    More Info

    • Introduction

      DNA repair protein complementing XP-A cells, (XPA), is a member of the XPA family. XPA protein takes a part in DNA excision repair. It Inductees repair by binding to damaged sites with different affinities depending on the photoproduct and the transcriptional state of the region. Defects in XPA is the reason of xeroderma pigmentosum complementation group A (XP-A), which is infrequent human autosomal recessive disease which characterized by solar sensitivity, high predisposition for developing cancers on areas exposed to sunlight, also may cause to neurological abnormalities.

    • Synonyms

      XP1, XPAC, DNA repair protein complementing XP-A cells.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human XPA mAb, clone PAT71H3, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human XPA protein 1-273 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT71H3AT.

    • Applications

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

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      XPA 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.

    Xpa Antibody
  • View Data Sheet

    Name :

    PSPN Mouse

    Description:

    Persephin Mouse Recombinant

    Persephin, PSPN.

    Product # :

    CYT-802

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    Description

    PSPN Mouse Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.7kDa. The PSPN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2?m filtered concentrated solution in 30 %ACN, 0.1 %TFA, 150mM NaCl.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg. 

    More Info

    • Introduction

      Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.

    • Synonyms

      Persephin, PSPN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG

    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.

    Pspn Mouse
  • View Data Sheet

    Name :

    Gly m 4.0101

    Description:

    Stress-Induced Protein SAM22 Recombinant

    Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

    Product # :

    PRO-2278

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    Description

    Recombinant Stress-Induced Protein SAM22 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 19,484 Dalton. Gly m 4.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Gly m 4.0101 is supplied in in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Stress-Induced Protein SAM22 (Gly m 4.0101) causes an allergic reaction in humans. Gly m 4 is the main soy allergen for patients allergic to birch pollen with soy allergy.

    • Synonyms

      Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    Gly M 40101
  • View Data Sheet

    Name :

    AMBP Human

    Description:

    Microglobulin Alpha-1 Protein Human

    Alpha-1 Microglobulin, A1M.

    Product # :

    PRO-407

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    Description

    Alpha 1-microglobulin (A1M) is an immunomodulatory protein with a broad spectrum of possible clinical applications and seems a promising marker for evaluation of tubular function.

    Source

    Purified from the urine of patients with chronic renal tubular proteinuria.

    Formulation

    Lyophilized from 0.02M NH4HCO3. May contain traces of buffer salts.

    Purity

    Greater than 96.0%.

    More Info

    • Introduction

      Alpha 1-microglobulin (A1M) is a lipocalin superfamily member (kernal lipocalins). A1M is a low molecular weight protein component of plasma. A1M is distributed in plasma and extravascular compartments of all organs. Alpha-1 Microglobulin is found in mammals, birds, amphibians and fish. The primary sites of A1M synthesis are the liver and the kidney. Around the opening of the lipocalin pocket three lysyl residues are situated; those residues carry yellow-brown modification derived from the binding and degradation of heme and kynurenin (a tryptophan metabolite). A1-Microglobulin’s reductase and dehydrogenase have broad biological substrate specificity properties due to its’ free cysteine side-chain which is located in a flexible loop. Alpha-1-microglobulin is glycosylated by three separate carbohydrate chains: two complex carbohydrates which are N-linked to asparagines at residues 17 and 96, and the other simple carbohydrate which is O-linked to threonine at position 5. The carbohydrates comprise 22% of the total molecular mass of the protein. The glycosylation varies between species. A1M exists in two forms- a free form and complexed to other macromolecules: in humans- complexed to immunoglobulin A (IgA), in rat- complexed to alpha-1-inhibitor-3. Free A1M is exceptionally heterogeneous in charge (therefore also known as protein HC), and is found tightly linked to a chromophore. The free Alpha-1-microglobulin is a monomeric protein composed of one 188 residue polypeptide and contains three cysteines, two of which (residues 75 and 173) form a conserved intra-molecular disulphide link. The chromophoric group is covalently bound to the free cysteine residue at position 34. A1M binds retinol as a major ligand, but this is probably distinct from its covalent chromophore. Half of all human plasma A1M (approximately 0.03mg/ml) forms a 1:1 complex with about 5% of plasma immunoglobulin A. The resulting macromolecular complexes’ molecular weight is 200000, and a plasma concentration of 0.3mg/ml. The complex can exhibit both antibody activity and affect many of the biological actions of free Alpha-1-microglobulin. Alpha-1-microglobulin was first discovered in pathological human urine. It was suggested that A1M might be involved in tissue defense against reactive oxygen species, oxidation by heme and kynurenin. Evidence also suggests that A1M functions in the regulation of the immune system. Other functions include: inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis.
      Other functions include inhibition of stimulation of cultured lymphocytes by protein antigens; induction of cell division of lymphocytes, a mitogenic effect that can either be enhanced or inhibited by the action of other plasma components; inhibition of neutrophil granulocyte migration in vitro; and inhibition of chemotaxis.

    • Synonyms

      Alpha-1 Microglobulin, A1M.

    • Physical Appearance

      Sterile Filtered Off-White lyophilized (freeze-dried) powder.

    • Stability

      Human A1M although stable at room temperature for 3 weeks, should be stored between 2-8°C.

    • Solubility

      Use phosphate buffer, pH>7.0 containing 0.15M NaCl, is recommended.

    • Human Virus Test

      Starting material tested and certified negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.

    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.

    Microglobulin Alpha 1 Human
  • View Data Sheet

    Name :

    Collagen-II Bovine

    Description:

    Bovine Collagen-II

    Product # :

    PRO-2679

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    Description

    Bovine Collagen-II is a natural protein purified from bovine knee joint. Collagen-II is purified by proprietary chromatographic techniques.

    Source

    Bovine knee joint.

    Formulation

    Collagen-II was lyophilized without additives.

    Purity

    > 95.0% .

    More Info

    • Introduction

      Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Collagen-II although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-II should be stored at 4C between 2-7 days and for future use below -18C.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 Add 50 mM acetic acid to prepare a working stock solution of approximately 1-5mg/ml and let the lyophilized pellet dissolve completely.

    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.

    Collagen Ii Bovine
  • View Data Sheet

    Name :

    SLC3A2 Human

    Description:

    Solute Carrier Family 3 Member 2 Human Recombinant

    Solute Carrier Family 3 Member 2, Lymphocyte Activation Antigen 4F2 Large Subunit, Solute Carrier Family 3 (Activators Of Dibasic And Neutral Amino Acid Transport), Member 2, Antigen Identified By Monoclonal Antibodies 4F2, TRA1.10, TROP4, And T43, Solute Carrier Family 3 (Amino Acid Transporter Heavy Chain), Member 2, 4F2 Cell-Surface Antigen Heavy Chain, Monoclonal Antibody 44D7, CD98 Heavy Chain, 4F2HC, MDU1, Antigen Defined By Monoclonal Antibody 4F2, Heavy Chain, Antigen Defined By Monoclonal Antibody 4F2, 4F2 Heavy Chain Antigen, 4F2 Heavy Chain, CD98 Antigen, Heavy Chain, CD98HC, 4T2HC, NACAE, CD98, 4F2, 4F2 cell-surface antigen heavy chain.

    Product # :

    PRO-2489

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    Description

    SLC3A2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 434 amino acids (206-630a.a.) and having a molecular mass of 47.9kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).SLC3A2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SLC3A2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SLC3A2, also known as Solute Carrier Family 3 Member 2, is a single-pass type II membrane protein which is part of the SLC3A transporter family. SLC3A2 is expressed ubiquitously in all tissues tested with the highest levels detected in kidney, placenta and testis and lowest level in thymus. SLC3A2 is essential for the function of light chain amino-acid transporters and also takes part in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. SLC3A2 participates in guiding and targeting of LAT1 and LAT2 to the plasma membrane.

    • Synonyms

      Solute Carrier Family 3 Member 2, Lymphocyte Activation Antigen 4F2 Large Subunit, Solute Carrier Family 3 (Activators Of Dibasic And Neutral Amino Acid Transport), Member 2, Antigen Identified By Monoclonal Antibodies 4F2, TRA1.10, TROP4, And T43, Solute Carrier Family 3 (Amino Acid Transporter Heavy Chain), Member 2, 4F2 Cell-Surface Antigen Heavy Chain, Monoclonal Antibody 44D7, CD98 Heavy Chain, 4F2HC, MDU1, Antigen Defined By Monoclonal Antibody 4F2, Heavy Chain, Antigen Defined By Monoclonal Antibody 4F2, 4F2 Heavy Chain Antigen, 4F2 Heavy Chain, CD98 Antigen, Heavy Chain, CD98HC, 4T2HC, NACAE, CD98, 4F2, 4F2 cell-surface antigen heavy chain.

    • 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

      ADPRAPRCRE LPAQKWWHTG ALYRIGDLQA FQGHGAGNLA GLKGRLDYLS SLKVKGLVLG PIHKNQKDDV AQTDLLQIDP NFGSKEDFDS LLQSAKKKSI RVILDLTPNY RGENSWFSTQ VDTVATKVKD ALEFWLQAGV DGFQVRDIEN LKDASSFLAE WQNITKGFSE DRLLIAGTNS SDLQQILSLL ESNKDLLLTS SYLSDSGSTG EHTKSLVTQY LNATGNRWCS WSLSQARLLT SFLPAQLLRL YQLMLFTLPG TPVFSYGDEI GLDAAALPGQ PMEAPVMLWD ESSFPDIPGA VSANMTVKGQ SEDPGSLLSL FRRLSDQRSK ERSLLHGDFH AFSAGPGLFS YIRHWDQNER FLVVLNFGDV GLSAGLQASD LPASASLPAK ADLLLSTQPG REEGSPLELE RLKLEPHEGL LLRFPYAAHH HHHH.

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

    Slc3A2 Human
  • View Data Sheet

    Name :

    EFNA1 Human, Sf9

    Description:

    Ephrin A1 Human Recombinant, Sf9

    Ephrin A1, Immediate Early Response Protein B61, TNF Alpha-Induced Protein 4, Ephrin-A1, TNFAIP4, LERK-1, EPLG1, LERK1, Tumor Necrosis Factor, Alpha-Induced Protein 4, Eph-Related Receptor Tyrosine Kinase Ligand 1, EPH-Related Receptor Tyrosine Kinase Ligand 1, Tumor Necrosis Factor Alpha-Induced Protein 4, Ligand Of Eph-Related Kinase 1, ECKLG, EFL1, B61, EPH-related receptor tyrosine kinase ligand 1, LERK-1.

    Product # :

    PRO-2538

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    Description

    EFNA1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 406 amino acids (19-182a.a.) and having a molecular mass of 46.6kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).EFNA1 is expressed with a 242 amino acid hIgG-His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EFNA1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      Ephrin A1, Immediate Early Response Protein B61, TNF Alpha-Induced Protein 4, Ephrin-A1, TNFAIP4, LERK-1, EPLG1, LERK1, Tumor Necrosis Factor, Alpha-Induced Protein 4, Eph-Related Receptor Tyrosine Kinase Ligand 1, EPH-Related Receptor Tyrosine Kinase Ligand 1, Tumor Necrosis Factor Alpha-Induced Protein 4, Ligand Of Eph-Related Kinase 1, ECKLG, EFL1, B61, EPH-related receptor tyrosine kinase ligand 1, LERK-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADPDRHTVFW NSSNPKFRNE DYTIHVQLND YVDIICPHYE DHSVADAAME QYILYLVEHE EYQLCQPQSK DQVRWQCNRP SAKHGPEKLS EKFQRFTPFT LGKEFKEGHS YYYISKPIHQ HEDRCLRLKV TVSGKITHSP QAHVNPQEKR LAADDPEVRV LHSIGHSLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH

    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.

    Ephrin A1
  • View Data Sheet

    Name :

    BLyS Human

    Description:

    B-cell Activating Factor Human Recombinant

    BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    Product # :

    CYT-307

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    Description

    BAFF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17007 Dalton. The BAFF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.0.

    Purity

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

    Biological Activity

    The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.

    More Info

    • Introduction

      BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
      B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
      Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.

    • Synonyms

      BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.

    • Background

      What is the molecular weight/Mw of BLYS Protein?
      BLYS Protein has a total Mw of 17.7kDa.

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

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

      What is the Biological Activity of BLYS Protein?
      The activity is determined by a mouse splenocyte survival assay. The ED50 for this effect is 0.5-2.0µg/ml.

      What is the amino acid sequence of BLYS Protein?
      MAVQGPEETV TQDCLQLIAD SETPTIQKGS YTFVPWLLSF KRGSALEEKE NKILVKETGY FFIYGQVLYT DKTYAMGHLI QRKKVHVFGD ELSLVTLFRC IQNMPETLPN NSCYSAGIAK LEEGDELQLA IPRENAQISL DGDVTFFGAL KLL.

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

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

    Blys Human
  • View Data Sheet

    Name :

    Inhibin alpha A Chain Human

    Description:

    Inhibin-Alpha A Chain Human Recombinant

    Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.

    Product # :

    HOR-293

    Price :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Inhibin-Alpha A chain Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids fragment (233-366) and having an amino-terminal hexahistidine tag, having a total molecular weight of 19.2 kDa. The Inhibin-Alpha A chain is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Inhibin-A alpha chain is supplied in 20mM Tris HCl (pH-8), 5mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    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.

    • Synonyms

      Inhibin-Alpha, A-Inhibin Subunit, Inhibin Alpha Chain, INHA.

    • 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.

    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 Alpha Chain Human
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