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Search results

1000 results found for “Hepatitis B”

Name

Description

Product #

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  • View Data Sheet

    Name :

    LTBR Human

    Description:

    Lymphotoxin Beta Receptor Human Recombinant

    Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.

    Product # :

    CYT-853

    Price :

    Quantity :

    Shipping Method :

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

    Description

    LTBR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 224 amino acids (28-227 a.a) and having a molecular mass of 24.6kDa.LTBR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LTBR protein solution (0.5mg/ml) containing PBS buffer (pH7.4) 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lymphotoxin Beta Receptor, also known as LTBR takes part in signaling during the development of lymphoid and other organs, lipid metabolism, immune response, and programmed cell death. In addition, the activity of this receptor has been associated to carcinogenesis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for LTBR.

    • Synonyms

      Lymphotoxin Beta Receptor (TNFR Superfamily, Member 3), TNFCR,Tumor Necrosis Factor Receptor 2-Related Protein,Tumor Necrosis Factor Receptor Type III, Tumor Necrosis Factor C Receptor,D12S370, TNFRSF3,TNFR3,Tumor Necrosis Factor Receptor Superfamily Member 3,Lymphotoxin-Beta Receptor,Lymphotoxin B Receptor, LT-BETA-R,TNF-R-III, TNFR2-RP, TNF-RIII,TNFR-III, TNFR-RP, CD18, LTBR.

    • 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 MGSMSQPQAV PPYASENQTC RDQEKEYYEP QHRICCSRCP PGTYVSAKCS RIRDTVCATC AENSYNEHWN YLTICQLCRP CDPVMGLEEI APCTSKRKTQ CRCQPGMFCA AWALECTHCE LLSDCPPGTE AELKDEVGKG NNHCVPCKAG HFQNTSSPSA RCQPHTRCEN QGLVEAAPGT AQSDTTCKNP LEPLPPEMSG TMLM

    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.

    Ltbr Human
  • View Data Sheet

    Name :

    HDGF2 Human

    Description:

    Hepatoma-Derived Growth Factor-2 Human Recombinant

    Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.

    Product # :

    CYT-132

    Price :

    Quantity :

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    • More Info
    • SDS-PAGE
    • Citations

    Description

    HDGF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-203 a.a.) and having a molecular mass of 25.1kDa (Molecular weight on SDS-PAGE will appear higher). HDGF2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HDGF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    SDS-PAGE

    HDGF2 Human - Product image 1

    Citations

    More Info

    • Introduction

      Hepatoma-derived growth factor, related protein 3 (HDGFRP3/HDGF2) is the original member of a family of polypeptides labeled HDGF related proteins (HRPs). The HDGF2 protein augments DNA synthesis and may play a part in cell proliferation. HDGF2 is expressed primarily in the testis and the brain, to an intermediate extent in the heart, and to a slight extent in the ovaries, kidneys, spleen, and liver in humans.

    • Synonyms

      Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.

    • 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 MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
      KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.

    • Background

      What is the molecular weight/Mw of HDGF2 HUMAN Protein?
      HDGF2 HUMAN Protein has a total Mw of 25.1kDa.

      What is the source or expression system of HDGF2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of HDGF2 HUMAN Protein?
      HDGF2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of HDGF2 HUMAN Protein?
      The biological functionality of HDGF2 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of HDGF2 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
      KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.

      What applications can HDGF2 HUMAN Protein be used in?
      HDGF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for HDGF2 HUMAN Protein?
      The endotoxin level is minimal, HDGF2 HUMAN 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.

    Hdgf2 Human
  • View Data Sheet

    Name :

    PON1 Human, HEK

    Description:

    Paraoxonase-1 Human Recombinant, HEK

    Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5

    Product # :

    ENZ-1154

    Price :

    Quantity :

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    • description
    • source
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    • biological activity
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    • Citations

    Description

    PON1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (16-355 a.a) containing a total of 346 amino acids, having a molecular mass of 39.0kDa. PON1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The PON1 solution (0.25mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,500 pmol/min/ug. Defined by the amount of enzyme that  hydrolyzes 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 37˚C.

    Citations

    More Info

    • Introduction

      Paraoxonase-1 or PON1 is part of the paraoxonase group of proteins. PON1 is an enzyme, responsible to the toxic metabolites of a different of organophosphorus insecticides hydrolyzation. Furthermore, PON1 is a dominant anti-atherosclerotic part of HDL. The enzyme needs PPAR-gamma for activation, leading to synthesis and release of paraoxonase 1 from the liver tissue, resulting in atherosclerosis reduction. PON1 has many qualities for atheroprotective through inflammatory lipid peroxides metabolism. This enzyme can hydrolyze a large number of substrates, for example cyclic carbonates, lactones, nerve gases etc.

    • Synonyms

      Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5

    • 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

      LFRNHQSSYQ TRLNALREVQ PVELPNCNLV KGIETGSEDL EILPNGLAFI SSGLKYPGIK SFNPNSPGKI LLMDLNEEDP TVLELGITGS KFDVSSFNPH GISTFTDEDN AMYLLVVNHP DAKSTVELFK FQEEEKSLLH LKTIRHKLLP NLNDIVAVGP EHFYGTNDHY FLDPYLQSWE MYLGLAWSYV VYYSPSEVRV VAEGFDFANG INISPDGKYV YIAELLAHKI HVYEKHANWT LTPLKSLDFN TLVDNISVDP ETGDLWVGCH PNGMKIFFYD SENPPASEVL RIQNILTEEP KVTQVYAENG TVLQGSTVAS VYKGKLLIGT VFHKALYCEL 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.

    Pon1 Enzyme
  • View Data Sheet

    Name :

    Leptin-B Tilapia

    Description:

    Leptin-B Tilapia Recombinant

    Product # :

    CYT-1110

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    Description

    Leptin-B Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 15,243 Dalton. The Leptin-B Tilapia is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.

    Purity

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

    Biological Activity

    Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.

    Citations

    More Info

    • Introduction

      Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      The first six N-terminal amino acids of recombinant Tilapia leptin B are Ala-Leu-Leu-Thr-Lys-Gly.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.19 for 1 mg/ml Leptin-B Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

    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 B
  • View Data Sheet

    Name :

    Bcl 2 Human (minus BH2 domain)

    Description:

    B-Cell Leukemia/Lymphoma 2 Human Recombinant (–BH2)

    Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

    Product # :

    PRO-632

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    Description

    Bcl-2 Des BH2 domain (187-202 residues) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 202 amino acids 1-186 and 203-218.The Bcl-2 is expressed as His-Tag fusion protein and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein 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.

    Citations

    More Info

    • Introduction

      BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.

    • Synonyms

      Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bcl-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bcl-2 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

      Suspend Bcl-2 in 100?l of 0.5M Acetic acid, over night at 4°C.
      Dilute 10 fold into selected buffer system.
      BCL-2 has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended.

    • Applications

      Input marker or positive control (Western Blotting).
      Function study.

    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.

    Bcl2 Human Des Bh2
  • View Data Sheet

    Name :

    MAX Human

    Description:

    MYC Associated Factor X Human Recombinant

    bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX Protein.

    Product # :

    PRO-811

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    Description

    MAX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-160 a.a.) and having a molecular mass of 19.3kDa. MAX protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    MAX Human solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MAX protein is part of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. MAX forms homodimers and heterodimers with Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms offers a complex system of transcriptional regulation. In contrast to Myc, which is exceedingly regulated throughout progression during the cell cycle, Max is very stable and is much more abundant than Myc.

    • Synonyms

      bHLHd4, bHLHd5, bHLHd6, bHLHd7, bHLHd8, MYC Associated Factor X, Class D basic helix-loop-helix protein 4, orf1, MGC10775, MGC11225, MGC18164, MGC34679, MGC36767, MAX 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

      MSDNDDIEVE SDEEQPRFQS AADKRAHHNA LERKRRDHIK DSFHSLRDSV PSLQGEKASR AQILDKATEY IQYMRRKNHT HQQDIDDLKR QNALLEQQVR ALEKARSSAQ LQTNYPSSDN SLYTNAKGST ISAFDGGSDS SSESEPEEPQ SRKKLRMEAS LEHHHHHH.

    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.

    Max Human
  • View Data Sheet

    Name :

    Shiga Like Toxin 2

    Description:

    Shiga Like Toxin-2 Subunit B Recombinant

    Product # :

    STX-002

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    Description

    Recombinant Shiga Like Toxin-2 Subunit B from E.Coli O157:H7 produced in E.coli having an Mw of 22kDa.The Shiga Like Toxin 2 protein is fused to a 6xHis tag at its N-terminus and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Shiga Like Toxin 2 protein solution contains PBS, 50mM arginine and 0.05% sodium azide.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    Citations

    More Info

    • Introduction

      Shiga-like toxin (verotoxin) is a toxin produced by some strains of Escherichia coli. Shiga-like toxin is named for its similarity to the AB5-type Shiga toxin produced by the bacteria Shigella dysenteriae. There are two known types-SLT1 and SLT2. The Shiga-like toxin is linked with hemolytic-uremic syndrome. Shiga-like toxin requires highly specific receptors on the cells' surface in order to attach and enter the cell. Species such as cattle, swine, and deer which do not carry these receptors may harbor toxigenic bacteria without any ill effect, dropping them in their feces, from where they may be distributed to humans. Shiga Like Toxin-2 Subunit B has nontoxic action, it is the functional region which binds to the receptor. Upon binding to the host cell receptor, the Shiga Like Toxin-2 Subunit B forms a pentamer. The Shiga Like Toxin-2 Subunit B can be useful in vaccine study, antibody test and other functional research.

    • 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.

    • Purification Method

      Purified by affinity 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.

    Shiga Like Toxin 2
  • View Data Sheet

    Name :

    MAO B Human

    Description:

    Monoamine Oxidase B Human Recombinant

    Amine oxidase [flavin-containing] B, Monoamine oxidase type B, MAO-B, MAOB, MGC26382.

    Product # :

    ENZ-440

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    Description

    MAO-B Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 488 amino acids fragment (2-489) corresponding to the cytoplasmic domain fragment of the mature protein, having a total molecular mass of 59.84kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The MAO-B is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MAO-B protein is supplied in 20mM Tris-HCl, pH 8.0, 250mM NaCl, 1mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MAO-B is a member of the flavin monoamine oxidase family. MAO-B (Monoamine oxidase B) is a flavin-containing mitochondrial enzyme that catalyzes the oxidative deamination of biogenic and xenobiotic monoamines. MAO-B controls the metabolic degradation of catecholamines and serotonin in neural and other target tissues. MAO-B is located in platelets and in DOPA-secreting neurons in the brain. MAOB and MAOA genes have an imperative function in DOPA degradation. Benzylamine and phenylethylamine are preferentially degraded by MAOB. The MAOB gene is linked to autistic traits, empathy and Asperger syndrome. Amplified levels of MAO B are identified in the brain of Alzheimer’s patients. High phenylethylamine levels in neonates as a result of low MAOB are consistent with phenylketonuria in newborns. Polymorphisms in MAO-B are connected to smoking behavior.

    • Synonyms

      Amine oxidase [flavin-containing] B, Monoamine oxidase type B, MAO-B, MAOB, MGC26382.

    • 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.

    Mao B Human
  • View Data Sheet

    Name :

    Bcl 2 Human (minus BH3 domain)

    Description:

    B-Cell Leukemia/Lymphoma 2 Human Recombinant (–BH3)

    Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

    Product # :

    PRO-633

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    Description

    Bcl-2 Des BH3 domain (93-107 residues) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids 1-92 and 108-218.The Bcl-2 is expressed as His-Tag fusion protein and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein 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.

    Citations

    More Info

    • Introduction

      BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.

    • Synonyms

      Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bcl-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bcl-2 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

      Suspend Bcl-2 in 100?l of 0.5M Acetic acid, over night at 4°C.
      Dilute 10 fold into selected buffer system.
      BCL-2 has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended.

    • Applications

      Input marker or positive control (Western Blotting).
      Function study.

    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.

    Bcl2 Human Des Bh3
  • View Data Sheet

    Name :

    Hepatocyte Growth Factor Human

    Description:

    Hepatocyte Growth Factor Human Recombinant

    Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.

    Product # :

    CYT-244

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    Description

    Hepatocyte Growth Factor Human Recombinant produced in Baculovirus is a heterodimer, non-glycosylated, polypeptide chain containing 697 a.a and having a total molecular mass of 78.0 KDa.The HGF is purified by proprietary chromatographic techniques.

    Source

    Insect cells.

    Formulation

    The sterile protein powder (1 mg/ml) is lyophilized from a solution containing 50mM acetic acid.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity was assayed for scattering activity in the MDCK cell assay. The ED50 for this effect is typically at 2.0-5.0 ng/ml.

    Citations

    More Info

    • Introduction

      Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3 and GM-CSF to stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.

    • Synonyms

      Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Hepatocyte Growth Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution HGF 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 Hepatocyte Growth Factor in 50mM acetic acid to a concentration not less than 100µg/ml. Further dilutions should be made using buffer containing protein.

    • Amino Acid Sequence

      QRKRRNTIHEFKKSAKTTLIKIDPALKIKTKKVNTADQCANRCTRNKGLPFTCK
      AFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYENKDYIRNCIIGKGRSYKGT
      VSITKSGIKCQPWSSMIPHEHSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRY
      EVCDIPQCSEVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPD
      KGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTCADNTMNDTDVPLETTECI
      QGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDGS
      ESPWCFTTDPNIRVGYCSQIPNCDMSHGQDCYRGNGKNYMGNLSQTRSGLTCSM
      WDKNMEDLHRHIFWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPISR
      CEGDTTPTIVNLDHPVISCAKTKQLRVVNGIPTRTNIGWMVSLRYRNKHICGGS
      LIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDEKCKQVLNVSQLVYGPEG
      SDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLR
      VAHLYIMGNEKCSQHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKM
      RMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKIILTYKVPQS.

    • Background

      What is the molecular weight/Mw of HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
      HEPATOCYTE GROWTH FACTOR HUMAN, Protein has a total Mw of 78kDa.

      What is the source or expression system of HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
      Insect cells.
      What is the Purity of HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
      HEPATOCYTE GROWTH FACTOR HUMAN, Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
      The activity was assayed for scattering activity in the MDCK cell assay. The ED50 for this effect is typically at 2.0-5.0 ng/ml.

      What is the amino acid sequence of HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
      QRKRRNTIHEFKKSAKTTLIKIDPALKIKTKKVNTADQCANRCTRNKGLPFTCK
      AFVFDKARKQCLWFPFNSMSSGVKKEFGHEFDLYENKDYIRNCIIGKGRSYKGT
      VSITKSGIKCQPWSSMIPHEHSYRGKDLQENYCRNPRGEEGGPWCFTSNPEVRY
      EVCDIPQCSEVECMTCNGESYRGLMDHTESGKICQRWDHQTPHRHKFLPERYPD
      KGFDDNYCRNPDGQPRPWCYTLDPHTRWEYCAIKTCADNTMNDTDVPLETTECI
      QGQGEGYRGTVNTIWNGIPCQRWDSQYPHEHDMTPENFKCKDLRENYCRNPDGS
      ESPWCFTTDPNIRVGYCSQIPNCDMSHGQDCYRGNGKNYMGNLSQTRSGLTCSM
      WDKNMEDLHRHIFWEPDASKLNENYCRNPDDDAHGPWCYTGNPLIPWDYCPISR
      CEGDTTPTIVNLDHPVISCAKTKQLRVVNGIPTRTNIGWMVSLRYRNKHICGGS
      LIKESWVLTARQCFPSRDLKDYEAWLGIHDVHGRGDEKCKQVLNVSQLVYGPEG
      SDLVLMKLARPAVLDDFVSTIDLPNYGCTIPEKTSCSVYGWGYTGLINYDGLLR
      VAHLYIMGNEKCSQHHRGKVTLNESEICAGAEKIGSGPCEGDYGGPLVCEQHKM
      RMVLGVIVPGRGCAIPNRPGIFVRVAYYAKWIHKIILTYKVPQS.What applications can

      HEPATOCYTE GROWTH FACTOR HUMAN, Protein be used in?
      HEPATOCYTE GROWTH FACTOR HUMAN, Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for HEPATOCYTE GROWTH FACTOR HUMAN, Protein?
      The endotoxin level is minimal, HEPATOCYTE GROWTH FACTOR HUMAN, 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.

    Hgf Human
  • View Data Sheet

    Name :

    TBEV preM

    Description:

    Tick-Borne Encephalitis Virus preM Recombinant

    Product # :

    TBE-287

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    Description

    The E.coli derived recombinant protein contains the Tick-borne Encephalitis Virus preM protein epitopes.

    Source

    Escherichia Coli.

    Formulation

    20mM MES pH 6.5, 8M urea, 200mM NaCl and 0.05% Tween-20.

    Purity

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

    Citations

    More Info

    • Introduction

      TBE is caused by tick-borne encephalitis virus (TBEV), a member of the family Flaviviridae.
      A closely related virus in Far Eastern Eurasia, Russian spring-summer encephalitis virus (RSSEV).
      The family Flaviviridae includes other tick-borne viruses are closely related to TBEV and RSSEV, such as Omsk hemorrhagic fever virus & Kyasanur Forest virus.
      Louping ill virus is also a member of this family.

    • Stability

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

    • Applications

      Encephalitis antigen is suitable for ELISA and Western blots, excellent antigen for detection of Tick-borne encephalitis virus with minimal specificity problems.

    • Specificity

      Immunoreactive with sera of encephalitis virus infected individuals.

    • Purification Method

      Encephalitis 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.

    Tbev Prem
  • View Data Sheet

    Name :

    EBV p18, GST

    Description:

    Epstein - Barr virus (HHV-4) p18 Recombinant, GST Tag

    Product # :

    EBV-277

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    Description

    The E.Coli derived recombinant protein contains the HHV-4 p18 regions, having a molecular mass of 35.4kDa which includes GST tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    3.8mg/ml in 50mM Tris-HCl, pH 8.0.

    Purity

    Protein is >90% pure as determined by 10% PAGE (coomassie staining).

    Citations

    More Info

    • Introduction

      The Epstein-Barr virus (EBV), also called Human herpes virus 4 (HHV-4), is a virus of the herpes family (which includes Herpes simplex virus and Cytomegalovirus. On infecting the B-lymphocyte, the linear virus genome circularizes and the virus subsequently persists within the cell as an episome. The virus can execute several distinct programs of gene expression which can be broadly categorized as being lytic cycle or latent cycle. The lytic cycle or productive infection results in staged expression of a host of viral proteins with the ultimate objective of producing infectious virions. Formally, this phase of infection does not inevitably lead to lysis of the host cell as EBV virions are produced by budding from the infected cell. The latent cycle (lysogenic) programs are those that do not result in production of virions. A very limited, distinct set of viral proteins are produced during latent cycle infection. These include Epstein-Barr nuclear antigen (EBNA)-1, EBNA-2, EBNA-3A, EBNA-3B, EBNA-3C, EBNA-leader protein (EBNA-LP) and latent membrane proteins (LMP)-1, LMP-2A and LMP-2B and the Epstein-Barr encoded RNAs (EBERs).

    • Stability

      EBV p18, GST although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      ASAGTGALAS SAPSTAVAQS ATPSVSSSIS SLRAATSGAT AAASAAAAVD TGSGGGGQPH DTAPRGARKK Q.

    • Purification Method

      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.

    Ebv P18 Gst
  • View Data Sheet

    Name :

    BAFFR Human, HEK

    Description:

    BAFF (BLyS) Receptor Human Recombinant, HEK

    TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.

    Product # :

    CYT-1224

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    Description

    BAFFR Human Recombinant is a single, glycosylated, polypeptide chain (1-78 a.a) containing a total of 314 amino acids and having a molecular mass of 34.4 kDa. BAFFR is fused to 233 a.a hIgG-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The BAFFR solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

    Citations

    More Info

    • Synonyms

      TNFRSF13C, CD268, BAFF-R, MGC138235, B cell-activating factor receptor.

    • 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

      DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.

    • Background

      B-cell Activating Factor (BAFF) and its corresponding receptor, BAFF-R, are integral components of the immune system, orchestrating crucial processes in B-cell survival, maturation, and differentiation. As we delve into the intricate world of immunology, the study of BAFF and its receptor has unveiled essential pathways that govern the immune responses in health and disease. This research investigates the multifaceted role of BAFF Receptor Protein, shedding light on its structural complexities, signaling mechanisms, and its pivotal contributions to immune regulation. By exploring the interactions between BAFF and its receptor, scientists aim to decipher the delicate balance that underlies immune homeostasis and explore potential therapeutic avenues.

      Structural Architecture of BAFF Receptor Protein:

      BAFF Receptor, a transmembrane protein predominantly expressed on B cells, belongs to the tumor necrosis factor receptor (TNFR) superfamily. Its intricate structure involves various domains, each playing a unique role in ligand binding, receptor activation, and downstream signaling. Understanding the structural intricacies of BAFF Receptor is paramount to unraveling the molecular events that govern B-cell fate decisions and immune responses.

      Physiological Significance in B-Cell Biology:

      BAFF Receptor, upon binding with its ligand BAFF, initiates a cascade of events critical for B-cell survival and function. This interaction promotes B-cell maturation, prevents premature apoptosis, and influences the formation of immune synapses. Additionally, BAFF Receptor signaling is tightly regulated to prevent excessive B-cell activation, ensuring immune tolerance and preventing autoimmune responses. Disruptions in these pathways can lead to autoimmune disorders, underscoring the crucial role of BAFF Receptor in maintaining immune equilibrium.

      Regulation of Immune Responses:

      BAFF Receptor signaling not only affects B-cell development but also has broader implications for immune responses. By modulating antibody production, B-cell activation, and immune memory, BAFF Receptor plays a vital role in shaping adaptive immunity. Its dysregulation has been implicated in various autoimmune conditions, making it an attractive target for therapeutic interventions aimed at restoring immune balance.

      BAFF Receptor as a Therapeutic Target:

      The intricate involvement of BAFF Receptor in autoimmune diseases, such as rheumatoid arthritis and systemic lupus erythematosus, has positioned it as a promising therapeutic target. Researchers are exploring monoclonal antibodies and other targeted therapies that aim to modulate BAFF Receptor signaling, providing a new frontier in autoimmune disease management. Additionally, understanding the BAFF-BAFF Receptor axis offers potential insights into the development of vaccines and immunotherapies, fostering innovative approaches in the fight against infectious diseases and malignancies.

      BAFF Receptor Protein, as a key player in immune regulation, embodies the complexities of immunology. Its interactions with BAFF orchestrate fundamental processes in B-cell biology and adaptive immunity. As scientists unravel the intricate signaling pathways and structural nuances of BAFF Receptor, they pave the way for novel therapeutic strategies and innovative treatments for autoimmune disorders and beyond. This research not only deepens our understanding of immune regulation but also holds the promise of transformative advancements in immunotherapy, ultimately shaping the future of immune-related healthcare.

      What is the molecular weight/Mw of BAFF-R Protein?
      BAFF-R Protein has a total Mw of 34.4kDa.

      What is the source or expression system of BAFF-R Protein?
      HEK293 Cells.

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

      What is the Biological Activity of BAFF-R Protein?
      The ED50 is ≤0.7 ug/ml, measured by its ability in a functional ELISA with BAFF Human.

      What is the amino acid sequence of BAFF-R Protein?
      DGSMRRGPRS LRGRDAPAPT PCVPAECFDL LVRHCVACGL LRTPRPKPAG ASSPAPRTAL QPQESVGAGA GEAALPLPGL LLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGK.

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

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

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    Baff Receptor Human
  • View Data Sheet

    Name :

    Borrelia p45

    Description:

    Borrelia Burgdorferi p45 Recombinant

    Product # :

    BOR-018

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    Description

    Recombinant Borrelia Burgdorferi p45 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 45,259.3 Dalton. Borrelia p45 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Borrelia p45 is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

    • 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.Immunodot test with Lyme disease positive/negative plasma, suitable for LTT (lymphocyte transformation test). 2.T cell stimulation assays. 3.ELISPOT (enzyme-linked immunospot).

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    Borrelia P45
  • 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.

    Citations

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    • 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 :

    HLA-DOB Human

    Description:

    Major Histocompatibility Complex Class II DO Beta Human Recombinant

    HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.

    Product # :

    PRO-1967

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    Description

    HLA-DOB Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (27-224) and having a molecular mass of 25.2 kDa.HLA-DOB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Major Histocompatibility Complex Class II DO Beta (HLA-DOB) is a part of the HLA class II beta chain paralogues. This class II beta chain is a heterodimer which is located in intracellular vesicles and consists of an alpha (DOA) and a beta chain (DOB), both anchored in the membrane. HLA-DOB which interacts with the HLA-DM molecule in B-cells is a significant modulator in the HLA class II restricted antigen presentation pathway. Class II molecules are expressed in antigen presenting cells such as B lymphocytes, dendritic cells and macrophages.

    • Synonyms

      HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.

    • 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 MGSGTDSPED FVIQAKADCY FTNGTEKVQF VVRFIFNLEE YVRFDSDVGM FVALTKLGQP DAEQWNSRLD LLERSRQAVD GVCRHNYRLG APFTVGRKVQ PEVTVYPERT PLLHQHNLLH CSVTGFYPGD IKIKWFLNGQ EERAGVMSTG PIRNGDWTFQ TVVMLEMTPE LGHVYTCLVD HSSLLSPVSV EWRAQSEYSW RK.

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    Hla Dob Human
  • View Data Sheet

    Name :

    HMBS Human

    Description:

    Hydroxymethylbilane Synthase Human Recombinant

    Porphobilinogen deaminase, PBG-D, Hydroxymethylbilane synthase, HMBS, Pre-uroporphyrinogen synthase, HMBS, PBGD, UPS, PORC.

    Product # :

    ENZ-581

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    Description

    HMBS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-361) and having a molecular mass of 41.9kDa.HMBS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HMBS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Porphobilinogen deaminase (HMBS) belongs to the hydroxymethylbilane synthase superfamily. HMBS is a cytoplasmic enzyme found in the heme synthesis pathway. HMBS is the 3rd enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of 4 porphobilinogen molecules into the linear hydroxymethylbilane. HMBS gene mutations cause errors in pyrrole metabolism which in turn lead to the autosomal dominant disease acute intermittent porphyria.

    • Synonyms

      Porphobilinogen deaminase, PBG-D, Hydroxymethylbilane synthase, HMBS, Pre-uroporphyrinogen synthase, HMBS, PBGD, UPS, PORC.

    • 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 MGSHMSGNGN AAATAEENSP KMRVIRVGTR KSQLARIQTD SVVATLKASY PGLQFEIIAM STTGDKILDT ALSKIGEKSL FTKELEHALE KNEVDLVVHS LKDLPTVLPP GFTIGAICKR ENPHDAVVFH PKFVGKTLET LPEKSVVGTS SLRRAAQLQR
      KFPHLEFRSI RGNLNTRLRK LDEQQEFSAI ILATAGLQRM GWHNRVGQIL HPEECMYAVG QGALGVEVRA KDQDILDLVG VLHDPETLLR CIAERAFLRH LEGGCSVPVA VHTAMKDGQL YLTGGVWSLD GSDSIQETMQ ATIHVPAQHE DGPEDDPQLV GITARNIPRG PQLAAQNLGI
      SLANLLLSKG AKNILDVARQ LNDAH.

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    Hmbs Human
  • View Data Sheet

    Name :

    BHMT Human

    Description:

    Betaine Homocysteine S-Methyltransferase Human Recombinant

    BHMT, Betaine Homocysteine S-Methyltransferase 1, BHMT1.

    Product # :

    ENZ-292

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    Description

    Betaine Homocysteine S-Methyltransferase Human Recombinant fused to His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 443 amino acids (21-236) and having a molecular mass of 49.2 kDa. The BHMT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BHMT solution contains 20mM Tris-HCl pH-7.5 and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Betaine-homocysteine methyltransferase (BHMT) is a cytosolic enzyme that catalyzes the conversion of betaine and homocysteine to dimethylglycine and methionine, respectively. BHMT displays differential expression in a model of liver cirrhosis.

    • Synonyms

      BHMT, Betaine Homocysteine S-Methyltransferase 1, BHMT1.

    • Physical Appearance

      Sterile Filtered clear colorless solution 1 mg/ml.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMPP VGGKKAKKGI LERLNAGEIV IGDGGFVFAL EKRGYVKAGP WTPEAAVEHP EAVRQLHREF LRAGSNVMQT FTFYASEDKL ENRGNYVLEK ISGQEVNEAA CDIARQVADE GDALVAGGVS QTPSYLSCKS ETEVKKVFLQ QLEVFMKKNV DFLIAEYFEH VEEAVWAVET LIASGKPVAA TMCIGPEGDL HGVPPGECAV RLVKAGASII GVNCHFDPTI SLKTVKLMKE GLEAARLKAH LMSQPLAYHT PDCNKQGFIDLPEFPFGLEP RVATRWDIQK YAREAYNLGV RYIGGCCGFE PYHIRAIAEE LAPERGFLPPASEKHGSWGS GLDMHTKPWV RARARKEYWE NLRIASGRPY NPSMSKPDGW GVTKGTAELM QQKEATTEQQ LKELFEKQKF KSQ.

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    Bhmt Human
  • View Data Sheet

    Name :

    MAVS Human

    Description:

    Mitochondrial Antiviral Signaling Protein Human Recombinant

    CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.

    Product # :

    PRO-1351

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    Description

    MAVS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 536 amino acids (1-513) and having a molecular mass of 55.9 kDa. MAVS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAVS solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Mitochondrial antiviral signaling protein (MAVS) is vital for innate immune defense against viruses. MAVS is an intermediary protein essential in the virus-triggered IFN-beta signaling pathways. MAVS is involved in activation of transcription factors that regulate expression of IFN-beta and contributes to antiviral immunity.

    • Synonyms

      CARDIF, IPS-1, IPS1, VISA, Mitochondrial antiviral-signaling protein, MAVS, Putative NF-kappa-B-activating protein 031N, Virus-induced-signaling adapter, KIAA1271.

    • 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 MGSMPFAEDK TYKYICRNFS NFCNVDVVEI LPYLPCLTAR DQDRLRATCT LSGNRDTLWH LFNTLQRRPG WVEYFIAALR GCELVDLADE VASVYQSYQP RTSDRPPDPL EPPSLPAERP GPPTPAAAHS IPYNSCREKE PSYPMPVQET QAPESPGENS EQALQTLSPR AIPRNPDGGP LESSSDLAAL SPLTSSGHQE QDTELGSTHT AGATSSLTPS RGPVSPSVSF QPLARSTPRA SRLPGPTGSV VSTGTSFSSS SPGLASAGAA EGKQGAESDQ AEPIICSSGA EAPANSLPSK VPTTLMPVNT VALKVPANPA SVSTVPSKLP TSSKPPGAVP SNALTNPAPS KLPINSTRAG MVPSKVPTSM VLTKVSASTV PTDGSSRNEE TPAAPTPAGA TGGSSAWLDS SSENRGLGSE LSKPGVLASQ VDSPFSGCFE DLAISASTSL GMGPCHGPEE NEYKSEGTFG IHVAENPSIQ LLEGNPGPPA DPDGGPRPQA DRKFQEREVP CHRPSP.

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    Mavs Human
  • View Data Sheet

    Name :

    CRYAB Human, His

    Description:

    Crystallin Alpha B Human Recombinant, His Tag

    CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    Product # :

    HSP-088

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    Description

    CRYAB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-175) and having a molecular mass of 21.2kDa. CRYAB is fused to an 8 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRYAB solution (1mg/ml) contains 10% glycerol & Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    • 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

      MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKKLEHHH HHH.

    • Background

      Alpha-B crystallin (CRYAB), a small heat shock protein, stands as a multifaceted molecular chaperone integral to cellular homeostasis and stress response. In its human recombinant form, CRYAB becomes a focal point in biomedical research, offering a controlled platform to explore its structural intricacies, cellular functions, and potential therapeutic applications. This research embarks on a comprehensive journey to unveil the diverse roles of CRYAB Human Recombinant, shedding light on its structural attributes, cellular interactions, and its implications in health and disease. By delving into the properties of CRYAB, scientists aim to deepen our understanding of cellular proteostasis and explore novel avenues in the treatment of protein misfolding disorders.

      Structural Insights into CRYAB Human Recombinant:

      CRYAB, forming oligomeric complexes, possesses a dynamic structural configuration crucial for its chaperone function. The human recombinant form, designed for controlled study, provides a unique window into the three-dimensional intricacies of CRYAB. Understanding its structure is fundamental for deciphering how CRYAB engages with client proteins, preventing their aggregation and maintaining cellular proteostasis.

      Cellular Functions in Proteostasis:

      As a molecular chaperone, CRYAB plays a pivotal role in preserving cellular proteostasis by preventing the aggregation of misfolded proteins. Beyond its chaperone function, CRYAB is implicated in diverse cellular processes, including modulation of apoptosis, regulation of cytoskeletal dynamics, and participation in cell signaling pathways. Elucidating the multifaceted functions of CRYAB Human Recombinant provides insights into its roles in health and disease.

      Implications in Neurodegenerative Disorders:

      CRYAB has garnered attention in the context of neurodegenerative disorders, where protein misfolding and aggregation are central pathological features. Studies involving CRYAB Human Recombinant have revealed its neuroprotective properties, suggesting its potential as a therapeutic target for conditions like Alzheimer's and Parkinson's diseases. Understanding the mechanisms by which CRYAB mitigates protein aggregation in neuronal cells holds promise for developing targeted interventions.

      CRYAB in Cardiovascular Health:

      The chaperone function of CRYAB extends to the cardiovascular system, where it safeguards against protein aggregation in cardiomyocytes. CRYAB Human Recombinant studies have illuminated its protective role in cardiac tissues, positioning it as a potential therapeutic avenue for heart diseases characterized by protein misfolding.

      Challenges and Future Directions:

      While the potential of CRYAB Human Recombinant in therapeutics is evident, challenges persist. Fine-tuning its applications, understanding its interactions with diverse client proteins, and exploring the intricacies of its roles in different cellular contexts are critical for translational success. Additionally, deciphering the specific mechanisms by which CRYAB contributes to the alleviation of protein misfolding disorders remains an active area of investigation.

      CRYAB Human Recombinant emerges as a linchpin in the cellular orchestra, orchestrating a symphony of functions vital for proteostasis. Its structural insights, diverse cellular functions, and therapeutic implications position it at the forefront of biomedical research. As researchers continue to unravel the molecular nuances of CRYAB, they not only deepen our understanding of cellular proteostasis but also pave the way for innovative treatments in neurodegenerative and cardiovascular disorders, shaping the future of precision medicine and protein folding therapeutics.

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    Cryab Human His
  • View Data Sheet

    Name :

    TNF B Human, Sf9

    Description:

    Tumor Necrosis Factor-beta Human Recombinant, Sf9

    Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.

    Product # :

    CYT-989

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    Description

    Tumor Necrosis Factor-beta Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 180 amino acids (35-205a.a.) and having a molecular mass of 19.7kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).TNFB is fused with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TNFB protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cytotoxicity assay using L-929 mouse fibrosarcoma cells in the presence of the metabolic inhibitor actinomycin D. The ED50 for this effect is ≤ 1ng/ml.

    Citations

    More Info

    • Introduction

      Lymphotoxin alpha, a member of the tumor necrosis factor family, is a cytokine produced by lymphocytes. LTA is highly inducible, secreted, and exists as homotrimeric molecule. LTA forms heterotrimers with lymphotoxin-beta which anchors lymphotoxin-alpha to the cell surface. LTA mediates a large variety of inflammatory, immunostimulatory, and antiviral responses. LTA is also involved in the formation of secondary lymphoid organs during development and plays a role in apoptosis.

    • Synonyms

      Lymphotoxin-alpha, LT-alpha, TNF-beta, Tumor necrosis factor ligand superfamily member 1, LTA, LT, TNFB, TNFSF1.

    • 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

      ADPLPGVGLT PSAAQTARQH PKMHLAHSTL KPAAHLIGDP SKQNSLLWRA NTDRAFLQDG FSLSNNSLLV PTSGIYFVYS QVVFSGKAYS PKATSSPLYL AHEVQLFSSQ YPFHVPLLSS QKMVYPGLQE PWLHSMYHGA AFQLTQGDQL STHTDGIPHL VLSPSTVFFG AFALHHHHHH.

    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.

    Tnfb Human Sf9
  • View Data Sheet

    Name :

    IL1B Mouse

    Description:

    Interleukin-1 beta Mouse Recombinant

    Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    Product # :

    CYT-273

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

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

    Description

    Interleukin-1 beta Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17500 Dalton. The IL-1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Mouse IL-1b was lyophilized from a sterile filtered aqueous solution in 10mM sodium phosphate, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity as determined by the dose-dependent proliferation of mouse D10S cells is 0.9-1.3pg/ml, corresponding to a Specific Activity of 1.1 x 106 Units/mg.

    Citations

    More Info

    • Introduction

      Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.

    • Synonyms

      Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1b 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-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MVPIRQLHYR LRDEQQKSLV LSDPYELKAL HLNGQNINQQ VIFSMSFVQGEPSNDKIPVA LGLKGKNLYL SCVMKDGTPT LQLESVDPKQ YPKKKMEKRFVFNKIEVKSK VEFESAEFPN WYISTSQAEH KPVFLGNNSG QDIIDFTMES VSS.

    • Background

      What is the molecular weight/Mw of IL1B MOUSE Protein?
      IL1B MOUSE Protein has a total Mw of 17.5kDa.

      What is the source or expression system of IL1B MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL1B MOUSE Protein?
      IL1B MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL1B MOUSE Protein?
      The activity as determined by the dose-dependent proliferation of mouse D10S cells is 0.9-1.3pg/ml, corresponding to a Specific Activity of 1.1 x 106 Units/mg.

      What is the amino acid sequence of IL1B MOUSE Protein?
      MVPIRQLHYR LRDEQQKSLV LSDPYELKAL HLNGQNINQQ VIFSMSFVQGEPSNDKIPVA LGLKGKNLYL SCVMKDGTPT LQLESVDPKQ YPKKKMEKRFVFNKIEVKSK VEFESAEFPN WYISTSQAEH KPVFLGNNSG QDIIDFTMES VSS.
      What applications can IL1B MOUSE Protein be used in?
      IL1B MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL1B MOUSE Protein?
      The endotoxin level is minimal, IL1B 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.

    Il 1 Beta Mouse
  • View Data Sheet

    Name :

    BD 1 Rat

    Description:

    Beta Defensin -1 Rat Recombinant

    Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.

    Product # :

    CYT-062

    Price :

    Quantity :

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

    Description

    BD-1 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 37 amino acids and having a molecular mass of 4.1kDa.The BD-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BD-1 protein was lyophilized from a 0.2µm filtered concentrated 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

    Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.

    Citations

    More Info

    • Introduction

      The Defensin family are highly similar in their protein sequence and are microbicidal & cytotoxic peptides made by neutrophils. Beta Defensin-1 is an antimicrobial peptide having the resistance of epithelial surfaces to microbial colonization. Beta Defensin-1 has close proximity to Defensin Alpha-1 and has been implicated in the pathogenesis of cystic fibrosis.
      Skin of patients having atopic dermatitis patients and mycosis fungoides (non-lesional and lesional) show lower human Beta Defensin-1 mRNA expression and higher human Beta Defensin-2 and human Beta Defensin-3 mRNA expression.
      Beta Defensin is highly expressed by epithelial cells.
      Beta-defensin 1 may play a role in the pathogenesis of severe sepsis.

    • Synonyms

      Beta-defensin 1, BD-1, rBD-1, Defensin beta 1, Defb1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BD-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 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 BD-1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.

    • Background

      What is the molecular weight/Mw of BD1 Protein?
      BD1 Protein has a total Mw of 4.1kDa.

      What is the source or expression system of BD1 Protein?
      Escherichia Coli.

      What is the Purity of BD1 Protein?
      BD1 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD1 Protein?
      Measured by its ability to chemoattract CD34+ dendritic cells using a concentration range of 0.1-1.0 ug/ml.

      What is the amino acid sequence of BD1 Protein?
      DQYRCLQNGG FCLRSSCPSH TKLQGTCKPD KPNCCRS.

      What applications can BD1 Protein be used in?
      BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD1 Protein?
      The endotoxin level is minimal, BD1 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.

    Bd 1 Rat
  • View Data Sheet

    Name :

    ARG2 Human

    Description:

    Arginase Type II Human Recombinant

    Kidney Arginase, Non-Hepatic Arginase, EC 3.5.3.1, Arginase-2, Type II arginase, Kidney-type arginase, Arginase-2 mitochondrial.

    Product # :

    ENZ-526

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

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

    Description

    ARG2 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (23-354 a.a.) and having a molecular mass of 38.3 kDa. The ARG2 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARG2 Human solution containing 20mM Tris-HCl pH-8, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ARG2 participates in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase. Since NO synthase is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, ARG2 takes part in both male and female sexual arousal and therefore a potential target for the treatment of male and female sexual arousal disorders.

    • Synonyms

      Kidney Arginase, Non-Hepatic Arginase, EC 3.5.3.1, Arginase-2, Type II arginase, Kidney-type arginase, Arginase-2 mitochondrial.

    • 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 MVHSVAVIGA PFSQGQKRKG VEHGPAAIRE AGLMKRLSSL GCHLKDFGDL SFTPVPKDDL YNNLIVNPRS VGLANQELAE VVSRAVSDGY SCVTLGGDHS LAIGTISGHA RHCPDLCVVW VDAHADINTP LTTSSGNLHG QPVSFLLREL QDKVPQLPGF SWIKPCISSA SIVYIGLRDV DPPEHFILKN YDIQYFSMRD IDRLGIQKVM ERTFDLLIGK RQRPIHLSFD IDAFDPTLAP ATFTPVVGGL TYREGMYIAE EIHNTGLLSA LDLVEVNPQL ATSEEEAKTT ANLAVDVIAS SFGQTREGGH IVYDQLPTPS SPDESENQAR VRI.

    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.

    Arg2 Human
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