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Search results

1000 results found for “Calbindin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    SERPIND1 Human

    Description:

    Serpin Peptidase Inhibitor, Clade D Member 1 Human Recombinant

    Serpin Family D Member 1, Cysteine Proteinase Inhibitor Clade D Member 1, Serpin Peptidase Inhibitor Clade D Member 1, Protease Inhibitor Leuserpin-2, Serpin D1, HCF2, HLS2, Leuserpin 2, D22S673, THPH10, HC-II, HCII, HC2, LS2.

    Product # :

    PRO-2050

    Price :

    Quantity :

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    • More Info

    Description

    SERPIND1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (58-499) and having a molecular mass of 53.3kDa.SERPIND1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SERPIND1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serpin Peptidase Inhibitor, Clade D Member 1 (SERPIND1) is a serine proteinase inhibitor which rapidly inhibits thrombin in the presence of dermatan sulfate. SERPIND1 gene is a member of the serpin gene superfamily. SERPIND1 protein contains 5 exons and 4 introns. SERPIND1 shares homology with antithrombin III and other members of the alpha 1-antitrypsin superfamily. SERPIND1 gene mutations are linked with cofactor II deficiency. SERPIND1 protein is activated by dermatan sulfate, and glycosaminoglycans. Allelic variations in the SERPIND1 gene are linked with cofactor II deficiency.

    • Synonyms

      Serpin Family D Member 1, Cysteine Proteinase Inhibitor Clade D Member 1, Serpin Peptidase Inhibitor Clade D Member 1, Protease Inhibitor Leuserpin-2, Serpin D1, HCF2, HLS2, Leuserpin 2, D22S673, THPH10, HC-II, HCII, HC2, LS2.

    • 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 MGSDFHKENT VTNDWIPEGE EDDDYLDLEK IFSEDDDYID IVDSLSVSPT DSDVSAGNIL QLFHGKSRIQ RLNILNAKFA FNLYRVLKDQ VNTFDNIFIA PVGISTAMGM ISLGLKGETH EQVHSILHFK DFVNASSKYE ITTIHNLFRK LTHRLFRRNF GYTLRSVNDL YIQKQFPILL DFKTKVREYY FAEAQIADFS DPAFISKTNN HIMKLTKGLI KDALENIDPA TQMMILNCIY FKGSWVNKFP VEMTHNHNFR LNEREVVKVS MMQTKGNFLA ANDQELDCDI LQLEYVGGIS MLIVVPHKMS GMKTLEAQLT PRVVERWQKS MTNRTREVLL PKFKLEKNYN LVESLKLMGI RMLFDKNGNM AGISDQRIAI DLFKHQGTIT VNEEGTQATT VTTVGFMPLS TQVRFTVDRP FLFLIYEHRT SCLLFMGRVA NPSRS.

    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.

    Serpind1 Human
  • View Data Sheet

    Name :

    Super Leptin qA Ovine

    Description:

    Super Leptin Antagonist Ovine Recombinant

    Product # :

    CYT-1245

    Price :

    Quantity :

    Shipping Method :

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    • source
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    Description

    Super Leptin Antagonist Ovine Recombinant is a single polypeptide chain containing 146 amino acids, an additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa. Super Ovine Leptin Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s super Ovine leptin antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Super Ovine leptin antagonist also inhibits various leptin effects in several in vitro bioassays.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Super Leptin Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 10, 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-Arg.

    • Background

      Leptin is a hormone which mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin receptors are expressed by various brain and peripheral cell types. leptin levels influence satiety, appetite and triggers behaviours which save energy. When leptin levels are high, the brain interprets that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. 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 Super Antagonist Ovine
  • View Data Sheet

    Name :

    GRXB E.Coli

    Description:

    Glutaredoxin-2 E.Coli Recombinant

    Glutaredoxin-2, Grx2, grxB, b1064, JW1051.

    Product # :

    ENZ-130

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    GRXB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 235 amino acids (1-215 a.a.) and having a molecular mass of 26.5kDa.GRXB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GRXB protein solution (1mg/ml) 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutaredoxin-2 (GrxB) is amember of the glutaredoxin family. Glutaredoxins are small redox enzymes of approximately 100 amino-acid residues which use glutathione as a cofactor. Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. GrxB is involved in reducing some disulfides in a coupled system with glutathione reductase. GrxB doesn’t act as hydrogen donor for ribonucleotide reductase.

    • Synonyms

      Glutaredoxin-2, Grx2, grxB, b1064, JW1051.

    • 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 MKLYIYDHCP YCLKARMIFG LKNIPVELHV LLNDDAETPT RMVGQKQVPI LQKDDSRYMP ESMDIVHYVD KLDGKPLLTG KRSPAIEEWL RKVNGYANKL LLPRFAKSAF DEFSTPAARK YFVDKKEASA GNFADLLAHS DGLIKNISDD LRALDKLIVK PNAVNGELSE DDIQLFPLLR NLTLVAGINW PSRVADYRDN MAKQTQINLL SSMAI.

    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.

    Grxb Ecoli
  • View Data Sheet

    Name :

    CA19-9 Human

    Description:

    CA19-9 Cancer Antigen Human

    Product # :

    PRO-2748

    Price :

    Quantity :

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    • description
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    • formulation
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    • More Info

    Description

    The Human CA19-9 Cancer Antigen is having a molecular mass of approximately 210kDa and was purified from human carcinoma cell line.

    Source

    Human carcinoma cell line.

    Formulation

    CA19-9 is supplied in a 0.05M sodium phosphate buffer, pH 7.5, 0.09% NaN3 and 1M NaCl and 5mM EDTA.

    Purity

    Greater than 60%.

    More Info

    • Introduction

      CA19-9 Cancer Antigen , aka CA19-9, is a cell surface glycoprotein complex most commonly associated with pancreatic ductal adenocarcinoma.
      The immunohistologic distribution of CA19-9 in tissues is consistent with the quantitative determination of higher CA19-9 concentrations in cancer than in normal or inflamed tissues. CA19-9 Cancer Antigen is a tumour marker raised in blood of patients with carcinoma of the gastro-intestinal tract.
      A declining Cancer Antigen CA19-9 value may be indicative of a favorable prognosis and good response to treatment.

    • Physical Appearance

      Clear colorless solution.

    • Stability

      Human CA19-9 although stable at 4°C for 1 week, should be stored at -20°C.

    • Human Virus Test

      Tissue sample tested and found negative for HIV-1 & 2 antibodies, HBsAg, and Hepatitis-C antibodies, Syphilis and HIV/HBV/HCV (PCR).

    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.

    Ca19 9 Human
  • View Data Sheet

    Name :

    Exenatide

    Description:

    Exenatide

    Exendin-4.

    Product # :

    HOR-246

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
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    Description

    Exenatide is a single, non-glycosylated, peptide containing 39 amino acids and having a molecular mass of 4186.6 Dalton. Exenatide has the empirical formula C184H282N50O60S.

    Formulation

    The Exenatide peptide was lyophilized from a concentrated solution with no additives.

    Purity

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

    More Info

    • Introduction

      Exenatide Derived from the saliva of the gila monster, is a 39 amino acid peptide that mimics the GLP-1 incretin, an insulin secretagogue with glucoregulatory effects. Typical responses to exenatide include improvements in the initial rapid release of endogenous insulin, suppression of glucagon release by the pancreas, regulation of gastric empyting, and reduced appetite - all of which function to lower blood glucose. Exenatide is self-regulating in that it lowers blood sugar when levels are elevated but does not continue to lower blood sugar when levels return to normal, unlike with sulfonylureas or insulins.

    • Synonyms

      Exendin-4.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      H-His-Gly-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Leu-Ser-Lys-Gln-Met-Glu-Glu-Glu-Ala-Val-Arg-Leu-Phe-Ile-Glu-Trp-Leu-Lys-Asn-Gly-Gly-Pro-Ser-Ser-Gly-Ala-Pro-Pro-Pro-Ser-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.

    Exenatide
  • View Data Sheet

    Name :

    CFB Human, Native

    Description:

    Complement Factor B Human

    CFB, C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, BF, BFD, AHUS4, ARMD14, CFAB, CFBD, FB, FBI12, GBG, H2-Bf.

    Product # :

    PRO-2698

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    Description

    Human Complement Factor B produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 93kDa.

    Source

    Human Plasma.

    Formulation

    CFB protein solution contains 10mM Sodium phosphate and 145mM NaCl, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.

    • Synonyms

      CFB, C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, BF, BFD, AHUS4, ARMD14, CFAB, CFBD, FB, FBI12, GBG, H2-Bf.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      CFB Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

    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.

    Complement Factor B Protein
  • View Data Sheet

    Name :

    DBI Mouse

    Description:

    Diazepam Binding Inhibitor Mouse Recombinant

    Acyl-CoA-binding protein, ACBP, Diazepam-binding inhibitor, DBI, Endozepine, EP, Dbi.  

    Product # :

    PRO-2527

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    Description

    DBI Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 110 amino acids (1-87 a.a) and having a molecular mass of 12.4kDa. DBI is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DBI protein solution (1mg/ml) contains Phosphate buffer saline (pH7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DBI, also known as Acyl-CoA-binding protein isoform 2, is a diazepam binding inhibitor, which is regulated by hormones. DBI participates in lipid metabolism and in the displacement of beta-carbolines & benzodiazepines, which modulate signal transduction at type A gamma-aminobutyric acid receptors located in brain synapses. Moreover, during adipocyte differentiation the expression of DBI is significantly induced. DBI preforms as an acyl-CoA pool former and regulates LCFA (long-chain fatty acids) metabolism in peripheral tissues.

    • Synonyms

      Acyl-CoA-binding protein, ACBP, Diazepam-binding inhibitor, DBI, Endozepine, EP, Dbi.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSQAEFD KAAEEVKRLK TQPTDEEMLF IYSHFKQATV GDVNTDRPGL LDLKGKAKWD SWNKLKGTSK ESAMKTYVEK VDELKKKYGI

    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.

    Dbi Mouse
  • View Data Sheet

    Name :

    Leptin Bovine

    Description:

    Leptin Bovine Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-502

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    Description

    Leptin Bovine 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 0.02% NaHCO3.

    Purity

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

    Biological Activity

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

    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 0.4% NaHCO3 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-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 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 Bovine
  • View Data Sheet

    Name :

    Leptin tA Ovine

    Description:

    Leptin Antagonist Triple Mutant Ovine Recombinant

    Product # :

    CYT-356

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    Description

    Leptin Antagonist Triple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

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

    Purity

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

    Biological Activity

    ProSpec’s Leptin-Antagonist Triple Mutant Ovine Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of mouse leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin-Antagonist Triple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, 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-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. 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 Ta Ovine
  • View Data Sheet

    Name :

    Avidin Recombinant

    Description:

    Avidin Recombinant

    Avidin, AVD, AVID.

    Product # :

    PRO-2597

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    Description

    Recombinant Avidin produced in Plants is a polypeptide chain having a molecular mass of 66kDa and 16kda per subunit. The Recombinant Avidin is purified by affinity chromatographic techniques.

    Source

    Corn (Zea Mays).

    Purity

    Greater than 90% as visualized by SDS-PAGE.

    Biological Activity

    13.5 units/mg protein, 1 unit binds 1µg biotin.

    More Info

    • Introduction

      Avidin is a tetrameric protein of 4 identical subunits (homotetramer) which can bind to biotin with a high degree of affinity and specificity. The estimated molecular weight of Avidin in its tetrameric form is between 66-69 kDa. Avidin is produced in the oviducts of birds, reptiles and amphibians and is subsequently deposited in the whites of their eggs. In the chicken egg white, avidin makes up roughly 0.05% of total protein (approximately 1.8 mg per egg). 10% of Avidin’s molecular weight is ascribed to carbohydrate content which is composed of 4-5 mannose and 3 N-acetylglucosamine residues. Avidin has at least three distinctive oligosaccharide structural type which are similar in structure and composition. The dissociation constant (KD) of avidin is approximately 10-15M, making it one of the strongest known non-covalent bonds.

    • Synonyms

      Avidin, AVD, AVID.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized Recombinant Avidin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Recombinant Avidin 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 Recombinant Avidin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml 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.

    Avidin Recombinant
  • View Data Sheet

    Name :

    CCL24 Mouse

    Description:

    Eotaxin-2 Mouse Recombinant (CCL24)

    C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    Product # :

    CHM-368

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    Description

    CCL24 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.3 kDa. The CCL24 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL24 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.15M sodium chloride.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
      CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3.

    • Synonyms

      C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Mouse Recombinant in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VTIPSSCCTS FISKKIPENR VVSYQLANGS ICPKAGVIFI TKKGHKICTD PKLLWVQRHI QKLDAKKNQP SKGAKAVRTK FAVQRRRGNS TEV.

    • Background

      What is the molecular weight/Mw of CCL24 MOUSE Protein?
      CCL24 MOUSE Protein has a total Mw of 10.3kDa.

      What is the source or expression system of CCL24 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL24 MOUSE Protein?
      CCL24 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL24 MOUSE Protein?
      Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL24 MOUSE Protein?
      VTIPSSCCTS FISKKIPENR VVSYQLANGS ICPKAGVIFI TKKGHKICTD PKLLWVQRHI QKLDAKKNQP SKGAKAVRTK FAVQRRRGNS TEV.

      What applications can CCL24 MOUSE Protein be used in?
      CCL24 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL24 MOUSE Protein?
      The endotoxin level is minimal, CCL24 MOUSE 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.

    Ccl24 Mouse
  • View Data Sheet

    Name :

    Cadherin-E Human

    Description:

    Cadherin-E Human Recombinant

    Epithelial cadherin, E-cadherin, Uvomorulin, Cadherin-1, CAM 120/80, CD324 antigen, CDH1, CDHE, UVO, ECAD, LCAM, Arc-1, CD324, Cadherin-E.

    Product # :

    PRO-461

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    Description

    Cadherin-E Human Recombinant (aa 600-707) expressed in E.coli, shows a 38 kDa band on SDS-PAGE.The Cadherin-E is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cadherin-E protein (100µg/1ml) in 50mM Tris-HCl, pH7.5 and 10mM L-glutathione (reduced).

    More Info

    • Introduction

      E-cadherin (uvomorulin, cell-CAM120/80) is a calcium dependent cell adhesion molecule expressed predominately in epithelial tissues. It plays an important role in the growth and development of cells via the mechanisms of control of tissue architecture and the maintenance of tissue integrity. Numerous studies have demonstrated that reduction and/or loss of Ecadherin expression in carcinomas correlates positively with the potential of these tumors for invasion and metastasis.

    • Synonyms

      Epithelial cadherin, E-cadherin, Uvomorulin, Cadherin-1, CAM 120/80, CD324 antigen, CDH1, CDHE, UVO, ECAD, LCAM, Arc-1, CD324, Cadherin-E.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      iffcernpkpq viniidadlp pntspftael thgasanwti qyndptqesi ilkpkmalev gdykinlklm dnqnkdqvtt levsvcdceg aagvcrkaqp veaglqi.

    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.

    E Cadherin Human
  • View Data Sheet

    Name :

    CFB-a Human

    Description:

    Complement Factor B Fragment a Human

    Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.

    Product # :

    PRO-2735

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    Description

    CFB-a Human produced in Human Plasma having a molecular mass of 33 kDa.

    Source

    Human Plasma.

    Formulation

    CFB-a solution (1mg/ml) contains Phosphate-buffered saline, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.

    • Synonyms

      Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      CFB-a Human is stable at 4°C if entire vial will be used within 2-4 weeks. Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

    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.

    Cfb Protein
  • View Data Sheet

    Name :

    ITGB3BP Human

    Description:

    Integrin Beta 3 Binding Protein Human Recombinant

    CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.

    Product # :

    PRO-1435

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    Description

    ITGB3BP Human Recombinant produced in E. coli is a single polypeptide chain containing 239 amino acids (1-216) and having a molecular mass of 27.1kDa. ITGB3BP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ITGB3BP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Integrin Beta 3 Binding Protein (ITGB3BP1) is a broadly expressed protein which contains a DD1 or RepD1 domain and an LXXLL motif. ITGB3BP1 functions as a nuclear receptor coactivator while induced by estrogen. ITGB3BP1 is also relates with the CENP-A-CAD complex that is engaged in mitotic progression, the assembly of kinetochore proteins and chromosome segregation. ITGB3BP1 behave s as a transcriptional corepressor via its interaction with the NFKB1 NF-kappa-B subunit by interfering with the transactivation domain of NFKB1.

    • Synonyms

      CENP-R, CENPR, HSU37139, NRIF3, TAP20, Centromere protein R, Beta-3-endonexin, Integrin beta-3-binding protein, Nuclear receptor-interacting factor 3, ITGB3BP.

    • 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 MGSMPFAPVA QARVQWHDFR SLQHLLPAFK RFSCLSLGSS WDYSVKRSLK LDGLLEENSF DPSKITRKKS VITYSPTTGT CQMSLFASPT SSEEQKHRNG LSNEKRKKLN HPSLTESKES TTKDNDEFMM LLSKVEKLSE EIMEIMQNLS SIQALEGSRE LENLIGISCA SHFLKREMQK TKELMTKVNK QKLFEKSTGL PHKASRHLDS YEFLKAILN.

    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.

    Itgb3Bp Human
  • View Data Sheet

    Name :

    TACSTD2 Human

    Description:

    Tumor-Associated Calcium Signal Transducer 2 Human Recombinant

    EGP-1, EGP1, GA733-1, GA7331, GP50, M1S1, TROP2, Cell surface glycoprotein Trop-2, Membrane component chromosome 1 surface marker 1, Pancreatic carcinoma marker protein GA733-1.

    Product # :

    PRO-157

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    Description

    TACSTD2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (31-274a.a.) and having a molecular mass of 29.9kDa. TACSTD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    TACSTD2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tumor-associated calcium signal transducer 2 (TACSTD2), is a member of to the EPCAM family. TACSTD2 is an intronless gene which encodes a carcinoma-associated antigen. TACSTD2 may act as a growth factor receptor and as a cell surface receptor that transduces calcium signals. Mutations of TACSTD2 have been associated with gelatinous drop-like corneal dystrophy.

    • Synonyms

      EGP-1, EGP1, GA733-1, GA7331, GP50, M1S1, TROP2, Cell surface glycoprotein Trop-2, Membrane component chromosome 1 surface marker 1, Pancreatic carcinoma marker protein GA733-1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSQDNCTCP TNKMTVCSPD GPGGRCQCRA LGSGMAVDCS TLTSKCLLLK ARMSAPKNAR TLVRPSEHAL VDNDGLYDPD CDPEGRFKAR QCNQTSVCWC VNSVGVRRTD KGDLSLRCDE LVRTHHILID LRHRPTAGAF NHSDLDAELR RLFRERYRLH PKFVAAVHYE QPTIQIELRQ NTSQKAAGDV DIGDAAYYFE RDIKGESLFQ GRGGLDLRVR GEPLQVERTL IYYLDEIPPK FSMKRLT.

    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.

    Tacstd2 Human
  • View Data Sheet

    Name :

    GDF6 Human

    Description:

    Bone Morphogenetic protein-13 Human Recombinant

    Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

    Product # :

    CYT-938

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    Description

    BMP13 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 120 amino acids and having a molecular mass of 27.1kDa.The BMP-13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-13 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

    More Info

    • Introduction

      Growth/differentiation factors (GDF1-GDF15) belong to the BMP family of TGF-beta superfamily proteins. These factors are produced as inactive preproproteins which are subsequently cleaved and assembled into active secreted homodimers. BMP13 is a growth factor which controls proliferation and cellular differentiation in the retina and bone formation. BMP13 has a central role in regulating apoptosis during retinal development. GDF proteins are vital during embryonic development, particularly in the skeletal, nervous, and muscular systems. BMP13 gene mutations result in colobomata, which are congenital abnormalities in ocular development, and in Klippel-Feil syndrome (KFS), which is a congenital disorder of spinal segmentation.

    • Synonyms

      Growth Differentiation Factor 6, Growth/Differentiation Factor 16, Bone Morphogenetic Protein 13, BMP-13, BMP13, GDF-6, Klippel-Feil Malformation, Segmentation Syndrome 1, Klip-Feil Malformation, Klippel-Feil Syndrome, MCOPCB6, SCDO4, CDMP2, LCA17, MCOP4, GDF16, KFS1, KFSL, SGM1, KFM, KFS, GDF6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP13 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-13 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 BMP13 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

    • Background

      Bone Morphogenetic Protein-13 Human Recombinant: Unraveling its Potential in Tissue Engineering and Regenerative Medicine

      Abstract:

      Bone Morphogenetic Protein-13 (BMP-13) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, regeneration, and repair. This research paper aims to provide a comprehensive analysis of BMP-13, including its characteristics, signaling pathways, and potential therapeutic applications. Furthermore, innovative methodologies for the production and optimization of BMP-13 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.

      Introduction:

      Tissue engineering and regenerative medicine hold great promise in addressing tissue repair and regeneration challenges. BMP-13, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the distinctive features of BMP-13 and presents novel approaches for the production and optimization of BMP-13 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-13 is a secreted growth factor belonging to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intricate intracellular signaling cascades. BMP-13 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate critical processes such as cell differentiation, proliferation, and extracellular matrix synthesis, influencing tissue development and repair.

      Production of BMP-13 Human Recombinant:

      Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-13 human recombinant. Various recombinant protein expression systems, such as mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-13. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-13 recombinant protein.

      Potential Therapeutic Applications:

      BMP-13 human recombinant holds immense promise in the field of tissue engineering and regenerative medicine. Its involvement in cartilage formation, osteogenesis, and tissue repair makes it a potential candidate for the treatment of musculoskeletal disorders, joint injuries, and cartilage defects. Furthermore, the ability of BMP-13 to modulate cell behavior and tissue remodeling indicates its wider therapeutic applications in diverse regenerative processes.

      Conclusion:

      BMP-13 human recombinant emerges as a crucial regulator in tissue engineering and regenerative medicine, offering significant potential for tissue repair and regeneration. Optimizing production methodologies and further unraveling its signaling mechanisms will undoubtedly enhance its therapeutic applications. Given its involvement in cartilage and bone formation, as well as tissue repair, BMP-13 human recombinant represents a valuable tool for promoting tissue regeneration and addressing the unmet clinical needs in regenerative medicine.

      What is the molecular weight/Mw of GDF6 Protein?
      GDF6 Protein has a total Mw of 27.1kDa.

      What is the source or expression system of GDF6 Protein?
      Escherichia Coli.

      What is the Purity of GDF6 Protein?
      GDF6 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF6 Protein?
      The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 2.0µg/ml, corresponding to a specific activity of > 500IU/mg.

      What is the amino acid sequence of GDF6 Protein?
      TAFASRHGKR HGKKSRLRCS KKPLHVNFKE LGWDDWIIAP LEYEAYHCEG VCDFPLRSHL EPTNHAIIQT LMNSMDPGST PPSCCVPTKL TPISILYIDA GNNVVYKQYE DMVVESCGCR.

      What applications can GDF6 Protein be used in?
      GDF6 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF6 Protein?

      The endotoxin level is minimal, GDF6 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.

    Bmp13 Human
  • View Data Sheet

    Name :

    CCL24 Rat

    Description:

    Eotaxin-2 Rat Recombinant (CCL24)

    C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    Product # :

    CHM-282

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    Description

    CCL24 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.2kDa. The CCL24 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
      CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3.

    • Synonyms

      C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Rat Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.

    • Background

      What is the molecular weight/Mw of CCL24 RAT Protein?
      CCL24 RAT Protein has a total Mw of 10.2kDa.

      What is the source or expression system of CCL24 RAT Protein?
      Escherichia Coli.

      What is the Purity of CCL24 RAT Protein?
      CCL24 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL24 RAT Protein?
      Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL24 RAT Protein?
      VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.

      What applications can CCL24 RAT Protein be used in?
      CCL24 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL24 RAT Protein?
      The endotoxin level is minimal, CCL24 RAT Protein was purified using conventional chromatography techniques.


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    Eotaxin 2 Rat
  • View Data Sheet

    Name :

    STC 2 Human, His

    Description:

    Stanniocalcin-2 Human Recombinant, His Tag

    Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.

    Product # :

    HOR-008

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    Description

    STC 2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 301 amino acids (25-302 a.a.) and having a molecular mass of 33kDa. STC 2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STC 2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.25M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      STC2 is a homodimeric glycoprotein that is expressed in a wide variety of tissues and may have autocrine or paracrine functions. The encoded protein has 10 of its 15 cysteine residues conserved among stanniocalcin family members and is phosphorylated by casein kinase 2 exclusively on its serine residues. Its C-terminus contains a cluster of histidine residues which may interact with metal ions. The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or cellular calcium/phosphate homeostasis. Constitutive over expression of human stanniocalcin 2 in mice resulted in pre- and postnatal growth restriction, reduced bone and skeletal muscle growth, and organomegaly. Expression of this gene is induced by estrogen and altered in some breast cancers.

    • Synonyms

      Stanniocalcin-2, STC, STC2, STCRP, STC-2, Stanniocalcin-related protein, STC-related protein.

    • 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 MGSTDATNPP EGPQDRSSQQ KGRLSLQNTA EIQHCLVNAG DVGCGVFECF ENNSCEIRGL HGICMTFLHN AGKFDAQGKS FIKDALKCKA HALRHRFGCI SRKCPAIREM VSQLQRECYL KHDLCAAAQE NTRVIVEMIH FKDLLLHEPY VDLVNLLLTC GEEVKEAITH SVQVQCEQNW GSLCSILSFC TSAIQKPPTA PPERQPQVDR TKLSRAHHGE AGHHLPEPSS RETGRGAKGE RGSKSHPNAH ARGRVGGLGA QGPSGSSEWE DEQSEYSDIR R.

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    Stc 2 Human His
  • View Data Sheet

    Name :

    CPPED1 Human

    Description:

    Calcineurin-Like Phosphoesterase Domain Containing 1 Human Recombinant

    CSTP1, Calcineurin-like phosphoesterase domain-containing protein 1, Complete S-transactivated protein 1, CPPED1.

    Product # :

    PRO-1500

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    Description

    CPPED1 Human Recombinant produced in E. coli is a single polypeptide chain containing 337 amino acids (1-314) and having a molecular mass of 37.9kDa. CPPED1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CPPED1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CPPED1 which is a part of the metallophosphoesterase superfamily takes part in glucose uptake by adipocytes. CPPED1 binds two divalent metal cations and is transactivated by the great envelope protein of the hepatitis B virus.

    • Synonyms

      CSTP1, Calcineurin-like phosphoesterase domain-containing protein 1, Complete S-transactivated protein 1, CPPED1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSAAEAG GVFHRARGRT LAAFPAEKES EWKGPFYFIL GADPQFGLIK AWSTGDCDNG GDEWEQEIRL TEQAVQAINK LNPKPKFFVL CGDLIHAMPG KPWRTEQTED LKRVLRAVDR AIPLVLVSGN HDIGNTPTAE TVEEFCRTWG DDYFSFWVGG VLFLVLNSQF YENPSKCPSL KQAQDQWLDE QLSIARQRHC QHAIVFQHIP LFLESIDEDD DYYFNLSKST RKKLADKFIH AGVKVVFSGH YHRNAGGTYQ NLDMVVSSAI GCQLGRDPHG LRVVVVTAEK IVHRYYSLDE LSEKGIEDDL MDLIKKK.

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    Cpped1 Human
  • View Data Sheet

    Name :

    S100A12 Human

    Description:

    S100 Calcium Binding Protein A12 Human Recombinant

    Extracellular newly identified RAGE-binding protein, Protein S100-A12, CGRP, Calcium-binding protein in amniotic fluid 1, CAAF1, Calgranulin-C, CAGC, EN-RAGE, Neutrophil S100 protein, S100 calcium-binding protein A12, p6, S100A12, MRP6, ENRAGE.

    Product # :

    PRO-152

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    Description

    The Recombinant Human S100A12 produced in E.coli has a molecular mass of 11.63kDa containing 101 amino acid residues of the human S100A12 and fused to a 10 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    S100A12 was filtered (0.4 µm) and lyophilized in 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

    More Info

    • Introduction

      S100A12 belongs to the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 family members are localized in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. S100A12 may be involved in specific calcium-dependent signal transduction pathways and its regulatory effect on cytoskeletal components may modulate various neutrophil activities.

    • Synonyms

      Extracellular newly identified RAGE-binding protein, Protein S100-A12, CGRP, Calcium-binding protein in amniotic fluid 1, CAAF1, Calgranulin-C, CAGC, EN-RAGE, Neutrophil S100 protein, S100 calcium-binding protein A12, p6, S100A12, MRP6, ENRAGE.

    • 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

      MKHHHHHHAS TKLEEHLEGI VNIFHQYSVR KGHFDTLSKG ELKQLLTKEL ANTIKNIKDK AVIDEIFQGL DANQDEQVDFQEFISLVAIA LKAAHYHTHK E.

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    S100A12 Human
  • View Data Sheet

    Name :

    SERPINA8 Human

    Description:

    Serpin Peptidase Inhibitor, Clade A Member 8 Human Recombinant

    Angiotensinogen, Serpin A8, AGT, SERPINA8, ANHU.

    Product # :

    PRO-1572

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    Description

    SERPINA8 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (a.a 34-485) containing a total of 462 amino acids, having a molecular mass of 51.0kDa (calculated) and fused to a 2 a.a C-terminal linker and an 8 a.a Flag tag at C-Terminus.The Human SERPINA8 is purified by proprietary chromatographic techniques.

    Source

    HEK 293.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serpin Peptidase Inhibitor, Clade A Member 8 (SERPINA8), which is a pre-angiotensinogen or angiotensinogen precursor, is expressed in the liver and cleaved by the enzyme renin in response to lowered blood pressure. The ensuing product, angiotensin I, is at that point cleaved by angiotensin converting enzyme (ACE) to produce the physiologically active enzyme angiotensin II. SERPINA8 protein is involved in maintaining blood pressure and in the pathogenesis of essential hypertension and preeclampsia. SERPINA8 gene mutations are linked with susceptibility to essential hypertension, and may cause renal tubular dysgenesis, which is a severe disorder of renal tubular development. Defects in the SERPINA8 gene are also linked with non-familial structural atrial fibrillation, and inflammatory bowel disease.

    • Synonyms

      Angiotensinogen, Serpin A8, AGT, SERPINA8, ANHU.

    • 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 a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. SERPINA8 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      DRVYIHPFHL VIHNESTCEQ LAKANAGKPK DPTFIPAPIQ AKTSPVDEKA LQDQLVLVAA KLDTEDKLRA AMVGMLANFL GFRIYGMHSE LWGVVHGATV LSPTAVFGTL ASLYLGALDH TADRLQAILG VPWKDKNCTS RLDAHKVLSA LQAVQGLLVA QGRADSQAQL LLSTVVGVFT APGLHLKQPF VQGLALYTPV VLPRSLDFTE LDVAAEKIDR FMQAVTGWKT GCSLTGASVD STLAFNTYVH FQGKMKGFSL LAEPQEFWVD NSTSVSVPML SGMGTFQHWS DIQDNFSVTQ VSFTESACLL LIQPHYASDL DKVEGLTFQQ NSLNWMKKLS PRTIHLTMPQ LVLQGSYDLQ DLLAQAELPA ILHTELNLQK LSNDRIRVGE VLNSIFFELE ADEREPTEST QQLNKPEVLE VTLNRPFLFA VYDQSATALH FLGRVANPLS TART DYKDDD DK.

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    Serpina8 Human
  • View Data Sheet

    Name :

    tBID Mouse

    Description:

    Truncated BH3 Interacting Domain Death Agonist Mouse Recombinant

    Truncated BH3-interacting domain death agonist, p22 BID, BID, FP497, MGC15319, MGC42355, tBID.

    Product # :

    PRO-644

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    Description

    Truncated BID Mouse Recombinant also called BH3-interacting domain death agonist p15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 61-195 amino acids (135 a.a.) and having a molecular mass of 15.4 kDa.

    Source

    Escherichia Coli.

    Formulation

    The Mouse Truncated BID protein solution contains 10mM Tris-HCl pH-8, 1mM EDTA and 250mM NaCl.

    Purity

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

    More Info

    • Introduction

      Truncated BH3 interacting domain death agonist is a truncated form of the pro-apoptotic full-length BID. Truncated BH3 interacting domain death agonist is generated by Caspase-8 cleavage of BID. The truncated form of the protein translocates from the cytosol to mitochondria and transduces apoptotic signals.
      BID is a pro-apoptotic Bcl-2 protein having only the BH3 domain. In reaction to apoptotic signaling, BID interacts with another Bcl-2 family of cell death regulators, called Bax, they form a heterodimer resulting to the insertion of Bax into the outer mitochondrial membrane. Bax induces the opening of the mitochondrial voltage-dependent anion channel which lead to the release of cytochrome c and other pro-apoptotic factors from the mitochondria resulting in activation of caspases. BID is a mediator of mitochondrial damage induced by caspase-8 (CASP8). CASP8 cleaves BID, and the COOH-terminal part translocates to mitochondria where it triggers cytochrome c release. The major proteolytic product p15 BID releasea cytochrome c. Isoform 1, Isoform 2 and Isoform 4 induce ice-like proteases and apoptosis while Isoform 3 does not induce apoptosis.

    • Synonyms

      Truncated BH3-interacting domain death agonist, p22 BID, BID, FP497, MGC15319, MGC42355, tBID.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • Stability

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

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    Tbid Mouse
  • View Data Sheet

    Name :

    Periostin Human, HEK

    Description:

    Periostin Human Recombinant, HEK

    OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    Product # :

    CYT-835

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    • More Info

    Description

    Periostin Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Asn22-Gln836) containing a total of 821 amino acids, having a calculated molecular mass of 91.8kDa and fused to a 6 aa His tag at C-Terminus.

    Source

    HEK 293.

    Formulation

    Periostin was filtered (0.4 µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5% trehalose.

    Purity

    Greater than 38.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Periostin is a disulfide linked 90 kDa, 811 amino acid protein originally isolated as a osteoblast-specific factor that functions as a cell adhesion molecule for preosteoblasts and is thought to be involved in osteoblast recruitment, attachment and spreading. Additionally, periostin expression has previously been shown to be significantly increased by both transforming growth factor beta-1(TGFbeta1) and bone morphogenetic protein (BMP-2). OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin
      Periostin mRNA is expressed in the developing mouse embryonic and fetal heart, and that it is localized to the endocardial cushions that ultimately divide the primitive heart tube into a four-chambered heart.

    • Synonyms

      OSF-2, Periostin, Osteoblast Specific Factor 2, PN OSF-2, PDLPOSTN, POSTN, MGC119510, MGC119511, PN, RP11-412K4.1.

    • 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.

    • 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. Periostin is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      NNHYDKILAH SRIRGRDQGP NVCALQQILG TKKKYFSTCK NWYKKSICGQ KTTVLYECCP GYMRMEGMKG CPAVLPIDHV YGTLGIVGAT TTQRYSDASK LREEIEGKGS FTYFAPSNEA WDNLDSDIRR GLESNVNVEL LNALHSHMIN KRMLTKDLKN GMIIPSMYNN LGLFINHYPN GVVTVNCARI IHGNQIATNG VVHVIDRVLT QIGTSIQDFI EAEDDLSSFR AAAITSDILE ALGRDGHFTL FAPTNEAFEK LPRGVLERIM GDKVASEALM KYHILNTLQC SESIMGGAVF ETLEGNTIEI GCDGDSITVN GIKMVNKKDI VTNNGVIHLI DQVLIPDSAK QVIELAGKQQ TTFTDLVAQL GLASALRPDG EYTLLAPVNN AFSDDTLSMD QRLLKLILQN HILKVKVGLN ELYNGQILET IGGKQLRVFV YRTAVCIENS CMEKGSKQGR NGAIHIFREI IKPAEKSLHE KLKQDKRFST FLSLLEAADL KELLTQPGDW TLFVPTNDAF KGMTSEEKEI LIRDKNALQN IILYHLTPGV FIGKGFEPGV TNILKTTQGS KIFLKEVNDT LLVNELKSKE SDIMTTNGVI HVVDKLLYPA DTPVGNDQLL EILNKLIKYI QIKFVRGSTF KEIPVTVYTT KIITKVVEPK IKVIEGSLQP IIKTEGPTLT KVKIEGEPEF RLIKEGETIT EVIHGEPIIK KYTKIIDGVP VEITEKETRE ERIITGPEIK YTRISTGGGE TEETLKKLLQ EEVTKVTKFI EGGDGHLFED EEIKRLLQGD TPVRKLQANK KVQGSRRRLR EGRSQHHHHH H.

    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.

    Periostin Human Hek
  • View Data Sheet

    Name :

    BEST1 Human

    Description:

    Bestrophin 1 Human Recombinant

    Bestrophin-1, TU15B, Vitelliform macular dystrophy protein 2, BEST1, VMD2, ARB, BEST, BMD, RP50, TU15B, Bestrophin-1 isoform 1, Bestrophin 1.

    Product # :

    PRO-1900

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    BEST1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (292-585) and having a molecular mass of 36 kDa.BEST1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BEST1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Bestrophin 1 (BEST1) is a part of the bestrophin gene family and is also forms calcium-activated chloride-ion channels in epithelial. This small gene family is characterized by proteins with a highly conserved N-terminus with 4-6 transmembrane domains. BEST1 is extremely permeable to bicarbonate.

    • Synonyms

      Bestrophin-1, TU15B, Vitelliform macular dystrophy protein 2, BEST1, VMD2, ARB, BEST, BMD, RP50, TU15B, Bestrophin-1 isoform 1, Bestrophin 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEQLINPF GEDDDDFETN WIVDRNLQVS LLAVDEMHQD LPRMEPDMYW NKPEPQPPYT AASAQFRRAS FMGSTFNISL NKEEMEFQPN QEDEEDAHAG IIGRFLGLQS HDHHPPRANS RTKLLWPKRE SLLHEGLPKN HKAAKQNVRG QEDNKAWKLK AVDAFKSAPL YQRPGYYSAP QTPLSPTPMF FPLEPSAPSK LHSVTGIDTK DKSLKTVSSG AKKSFELLSE SDGALMEHPE VSQVRRKTVE FNLTDMPEIP ENHLKEPLEQ SPTNIHTTLK DHMDPYWALE NRDEAHS.

    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.

    Best1 Human
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