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Search results

1000 results found for “aprotinin”

Name

Description

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  • View Data Sheet

    Name :

    ARL4A Human

    Description:

    ADP-Ribosylation Factor-Like 4A Human Recombinant

    ADP-ribosylation factor-like protein 4A, ARL4A.

    Product # :

    PRO-895

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    • More Info

    Description

    ARL4A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (1-200) and having a molecular mass of 24.7 kDa.The ARL4A is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ARL4A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ARL4A is related Specifically to ARL6 and ARL7 and belongs to the ARF-like protein (ARL) subfamily of small GTPases. However, unlike ARFs, ARL4 does not activate the cholera toxin ADP-ribosyltranferase. ARL4A takes part in neurogenesis during embryonic development and somitogenesis in the early stages of adult spermatogenesis.

    • Synonyms

      ADP-ribosylation factor-like protein 4A, ARL4A.

    • 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 MGNGLSDQTS ILSNLPSFQS FHIVILGLDC AGKTTVLYRL QFNEFVNTVP TKGFNTEKIK VTLGNSKTVT FHFWDVGGQE KLRPLWKSYT RCTDGIVFVV DSVDVERMEE AKTELHKITR ISENQGVPVL IVANKQDLRN SLSLSEIEKL LAMGELSSST PWHLQPTCAI IGDGLKEGLE KLHDMIIKRR KMLRQQKKKR

    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.

    Arl4A Human
  • View Data Sheet

    Name :

    Noggin Human

    Description:

    Noggin Human Recombinant

    SYM1, SYNS1, NOG.

    Product # :

    CYT-475

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
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    • More Info

    Description

    Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED50 for this effect  is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x105units/mg.

    More Info

    • Introduction

      The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

    • Synonyms

      SYM1, SYNS1, NOG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
      EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
      RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
      TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC.

    • Background

      Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.

      Abstract:

      Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.

      Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.

      This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.

      Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      1. Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.

      Molecular Characteristics of Noggin :

      1. This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.

      Inhibition of BMP Signaling by Noggin:

      1. Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.

      Physiological Functions of Noggin:

      1. Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.

      Therapeutic Implications of Noggin:

      1. The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.

      Clinical Studies and Translational Research:

      1. This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical studies.

    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.

    Noggin Human
  • View Data Sheet

    Name :

    Omentin Human, His

    Description:

    Omentin Human Recombinant, His Tag

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

    Product # :

    CYT-551

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    • More Info

    Description

    Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 294 amino acids and having a molecular mass of 32.7 kDa. Recombinant Human Omentin contains His tag fused at N-Terminus.Intelectin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of lyophilized powder contains 20mM Tris & 50mM NaCl pH-8.0.

    Purity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASTDEANT YFKEWTCSSS PSLPRSCKEI KDECPSAFDG LYFLRTENGV IYQTFCDMTS GGGGWTLVAS VHENDMRGKC TVGDRWSSQQ GSKAVYPEGD GNWANYNTFG SAEAATSDDY KNPGYYDIQA KDLGIWHVPN KSPMQHWRNS SLLRYRTDTG FLQTLGHNLF GIYQKYPVKY GEGKCWTDNG PVIPVVYDFG DAQKTASYYS PYGQREFTAG FVQFRVFNNE RAANALCAGM RVTGCNTEHH CIGGGGYFPE ASPQQCGDFS GFDWSGYGTH VGYS.

    • Applications

      Elisa
      Western blot.

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

    Omentin Human His
  • View Data Sheet

    Name :

    Osteocrin Human

    Description:

    Osteocrin Human Recombinant

    Osteocrin, Musclin, OSTN.

    Product # :

    PRO-420

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
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    Description

    The recombinant Human Osteocrin is produced with N-terminal fusion of His Tag. The Human Osteocrin His-Tagged Fusion Protein is 13.6 kDa containing 106 amino acid residues of the human Osteocrin and 16 additional amino acid residues – His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer, pH 4.0.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Osteocrin is a recently identified secreted protein expression of which was only detected in bone, peaking just after birth and decreasing markedly with age. A 1280-bp mRNA encodes osteocrin producing a mature protein of 103 amino acids with a molecular mass of 11.4 kDa. In primary osteoblastic cell cultures osteocrin expression coincided with matrix formation then decreased in very mature cultures. Treatment of cultures with 1,25-dihydroxyvitamin D3 resulted in a rapid dose- dependent down-regulation of osteocrin expression, suggesting direct regulation. Chronic treatment of primary cultures with osteocrin-conditioned media inhibited mineralization and reduced osteocalcin and alkaline phosphatase expression. These results suggest that osteocrin represents a novel, unique vitamin D-regulated bone-specific protein that appears to act as a soluble osteoblast regulator.

    • Synonyms

      Osteocrin, Musclin, OSTN.

    • 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 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMVDVT TTEAFDSGVI DVQSTPTVRE EKSATDLTAK LLLLDELVSL ENDVIETKKK RSFSGFGSPL DRLSAGSVDH KGKQRKVVDH PKRRFGIPMD RIGRNRLSNS RG.

    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.

    Musclin Human
  • View Data Sheet

    Name :

    PFN2 Human

    Description:

    Profilin-2 Human Recombinant

    Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.

    Product # :

    PRO-809

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    Description

    PFN2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.2 kDa. PFN2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PFN2 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PFN2 is a ubiquitous actin monomer-binding protein which is part of the profilin family. PFN2 regulates actin polymerization in response to extra cellular signals. PFN2 binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, while it increases it at low concentrations. PFN2 binds to PIP2, it inhibits the formation of IP3 and DG.

    • Synonyms

      Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.

    • 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 MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM IVGKDREGFF TNGLALGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH GGGLNKKAYS MAKYLRDSGF.

    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.

    Pfn2 Human
  • View Data Sheet

    Name :

    PRDX3 Human

    Description:

    Peroxiredoxin-3 Human Recombinant

    AOP1, MER5, AOP-1, SP-22, PRO1748, MGC24293, MGC104387, PRDX3, Thioredoxin-dependent peroxide reductase mitochondrial, Peroxiredoxin-3, PRX III, Antioxidant protein 1, Protein MER5 homolog, HBC189.

    Product # :

    ENZ-419

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    Description

    PRDX3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids (63-256 a.a.) and having a molecular mass of 21.5 kDa.The PRDX3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PRDX3 solution contains 20mM Tris-HCl pH-8, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be approximately 82-83 pmole/min/µg.
    The enzymatic activity was confirmed by measuring the remaining peroxide after incubation of PRDX3 and peroxide for 20 min at room temperature. Specific activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25°C for 1 minute.

    More Info

    • Introduction

      PRDX3 is part of the peroxiredoxin family of antioxidant enzymes, that reduces hydrogen peroxide and alkyl hydroperoxides. PRDX3 is particularly located in the mitochondria and involved in the regulation of cellular redox status by serving as a primary line of defense against H2O2 produced during respiration. PRDX3 is a significant regulator of the abundance of mitochondrial H(2)O(2), which itself promotes apoptosis in cooperation with other mediators of apoptotic signaling. PRDX3 mitochondrial protein is significantly decreased in Alzheimer Disease and Down Syndrome.

    • Synonyms

      AOP1, MER5, AOP-1, SP-22, PRO1748, MGC24293, MGC104387, PRDX3, Thioredoxin-dependent peroxide reductase mitochondrial, Peroxiredoxin-3, PRX III, Antioxidant protein 1, Protein MER5 homolog, HBC189.

    • 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

      MPAVTQHAPY FKGTAVVNGE FKDLSLDDFK GKYLVLFFYP LDFTFVCPTE IVAFSDKANE FHDVNCEVVA VSVDSHFSHL AWINTPRKNG GLGHMNIALL SDLTKQISRD YGVLLEGSGL ALRGLFIIDP NGVIKHLSVN DLPVGRSVEE TLRLVKAFQY VETHGEVCPA NWTPDSPTIK PSPAASKEYF QKVNQ.

    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.

    Prdx3 Human
  • View Data Sheet

    Name :

    LHRH Protein

    Description:

    Luteinizing Hormone Releasing Hormone Human Recombinant

    LHRH, GRH, GNRH, LNRH.

    Product # :

    HOR-268

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    Description

    LHRH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 92 amino acids (24-92 a.a.) and having a molecular mass of 10.3kDa.LHRH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GNRH1 also known as Luteinising-hormone releasing hormone (LHRH), is a peptide hormone responsible for the release of FSH and LH from the anterior pituitary. GNRH1 is synthesized and released by the hypothalamus.
      At the pituitary, GNRH1 stimulates the synthesis and secretion of the follicle-stimulating hormone (FSH) and luteinizing hormone (LH). These processes are controlled by the size and frequency of GNRH1 pulses, as well as by feedback from androgens and estrogens. Low requency GNRH1 pulses lead to FSH release, whereas high frequency GNRH1 pulses stimulate LH release.
      There are differences in GNRH1 secretion between males and females. In males, GNRH1 is secreted in pulses at a constant frequency, but in females the frequency of the pulses varies during the menstrual cycle and there is a large surge of GNRH1 just before ovulation.
      GNRH1 secretion is pulsatile in all vertebrates, and is necessary for correct reproductive function. Thus, a single hormone, GNRH1, controls a complex process of follicular growth, ovulation, and corpus luteum maintenance in the female, and spermatogenesis in the male.

    • Synonyms

      LHRH, GRH, GNRH, LNRH.

    • 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 MGSQHWSYGL RPGGKRDAEN LIDSFQEIVK EVGQLAETQR FECTTHQPRS PLRDLKGALE SLIEEETGQK KI.

    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.

    Lhrh Human Recombinant
  • View Data Sheet

    Name :

    Clusterin

    Description:

    Human Clusterin

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

    Product # :

    CYT-548

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    Source

    Plasma.

    Formulation

    Human native Clusterin was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.1M phosphate buffer, 0.15M NaCl pH 7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized Clusterin 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 H2O to prepare a working stock solution of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

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

    Clusterin Human
  • View Data Sheet

    Name :

    APOH Bovine

    Description:

    Apoliporotein-H Bovine

    Beta-2-glycoprotein 1, Apolipoprotein H, Apo-H, Beta-2-glycoprotein I, B2GPI, Beta(2)GPI, APOH.

    Product # :

    PRO-1504

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    Description

    Bovine Apolipoprotein-H polypeptide is purified from fetal calf serum (FCS) by proprietary protein-chemical techniques, having an Mw of approximately 70kDa.

    Source

    Fetal calf serum (FCS).

    Formulation

    APOH protein solution is supplied in 16mM Tris-HCl pH-8.0, 280mM NaCl, 0.16mM AEBSF and 20% glycerol.

    Purity

    Greater than 70% as determined by SDS-PAGE.

    More Info

    • Introduction

      Apolipoprotein H (APOH) attaches to numerous kinds of negatively charged substances for instance phospholipids, and dextran sulfate. APOH prevents activation of the intrinsic blood coagulation cascade by attaching to phospholipids on the surface of damaged cells. APOH expressed by the liver and secreted in the plasma.

    • Synonyms

      Beta-2-glycoprotein 1, Apolipoprotein H, Apo-H, Beta-2-glycoprotein I, B2GPI, Beta(2)GPI, APOH.

    • 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.

    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.

    Apoh Bovine
  • View Data Sheet

    Name :

    ProInsulin Human

    Description:

    ProInsulin C-Peptide Analogue Human Recombinant

    Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN. 

    Product # :

    CYT-1120

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    Description

    ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.ProInsulin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    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.

    More Info

    • Introduction

      Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.

    • Synonyms

      Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ProInsulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProInsulin C-Peptide Analogue should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized ProInsulin C-Peptide Analogue in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR.

    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.

    Proinsulin C Peptide
  • View Data Sheet

    Name :

    Transferrin Human, CHO

    Description:

    Transferrin Human Recombinant, CHO

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

    Product # :

    PRO-2782

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    Description

    Recombinant Human Transferrin produced in CHO cells is a glycosylated, polypeptide chain containing having a molecular mass of 76 kDa. Human Transferrin has homologous C and N-terminal domains, each of which binds one ion of ferric iron.

    Source

    Chinese Hamster Ovary cells.

    Formulation

    Transferrin solution contains 0.05% NaN3 and PBS.

    Purity

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

    More Info

    • Synonyms

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

    • 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.

    • Applications

      Immunoassay, cell culture.

    • Background

      Human recombinant transferrin, a glycoprotein responsible for iron transport in the body, has gained increasing attention in the fields of biomedicine and health sciences. This multifaceted protein serves as an essential carrier of iron and is crucial for cellular growth, immunity, and various physiological processes. Its recombinant form, produced through advanced biotechnological methods, offers several advantages for therapeutic and research purposes. This study aims to provide a comprehensive exploration of human recombinant transferrin, shedding light on its various functions and potential applications in health and biomedicine.

      The primary objective of this research is to elucidate the essential role of transferrin in iron homeostasis and its significance for human health. In vitro and in vivo experiments will be conducted to investigate how recombinant transferrin interacts with cellular receptors, regulates iron uptake, and influences cellular proliferation. Understanding these mechanisms is fundamental for deciphering the complexities of iron metabolism and its impact on health and disease.

      The second objective is to assess the clinical relevance of human recombinant transferrin in medical interventions. Clinical trials and studies involving individuals with iron-related disorders, such as iron-deficiency anemia, will be conducted to evaluate the efficacy and safety of recombinant transferrin supplementation. These investigations may provide insights into the use of recombinant transferrin as a therapeutic agent in various clinical settings.

      The third objective is to explore the broader implications of human recombinant transferrin in biomedicine and research. Research will investigate its potential roles in areas beyond iron transport, such as drug delivery, tissue engineering, and cell culture. Understanding the multifaceted properties of recombinant transferrin may open new avenues for innovative approaches in various medical specialties and scientific research.

      By delving into the diverse functions of human recombinant transferrin, this research aims to expand our understanding of its physiological roles and clinical applications. The findings may contribute to the development of innovative strategies for the treatment of iron-related disorders and the advancement of biomedicine and scientific research.

    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.

    Transferrin Protein
  • View Data Sheet

    Name :

    AIFM1 Antibody

    Description:

    Apoptosis-Inducing Factor Mitochondrion-Associated 1, Mouse Anti Human

    Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 1.

    Product # :

    ANT-634

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    Formulation

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

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    • Introduction

      Apoptosis-Inducing Factor, Mitochondrion-Associated, 1 (AIFM1) is a mitochondrial protein which translocates to the nucleus once apoptosis has been initiated. AIFM1 causes DNA fragmentation and chromatin condensation and also triggers the release of cytochrome c and caspase-9 from mitochondria. Bcl-2 overexpression prevents the release of AIFM1 from mitochondria, but doesn’t block its apoptogenic activity.

    • Synonyms

      Apoptosis-inducing factor 1, mitochondrial, Programmed cell death protein 8, AIFM1, AIF, PDCD8, CMTX4, COWCK, COXPD6, isoform 2 precursor, Apoptosis-Inducing Factor, Mitochondrion-Associated, 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human AIFM1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human AIFM1 protein 98-609 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and k light chain.

    • Clone

      PAT22E9AT.

    • Applications

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

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    • Purification Method

      AIFM1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Aifm1 Antibody
  • View Data Sheet

    Name :

    Leptin Human

    Description:

    Human Leptin

    OB Protein, Obesity Protein, OBS, Obesity factor, Leptin.

    Product # :

    CYT-683

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    Description

    Leptin Human produced syntheticaly contains 35 amino acids (22-56 a.a.) having a molecular mass of 3950.6 Dalton.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

    Purity

    Greater than 95.0% as determined by RP-HPLC.

    More Info

    • Introduction

      A 16kDa 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, Leptin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin although stable at room temperature, should be stored desiccated below -20°C. Reconstituted Leptin is best stored refrigerated at 4°C.

    • Solubility

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

    • Amino Acid Sequence

      Val-Pro-Ile-Gln-Lys-Val-Gln-Asp-Asp-Thr-Lys-Thr-Leu-Ile-Lys-Thr-Ile-Val-Thr-Arg-Ile-Asn-Asp-Ile-Ser-His-Thr-Gln-Ser-Val-Ser-Ser-Lys-Gln-Lys.

    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 Synthetic
  • View Data Sheet

    Name :

    Protein G

    Description:

    Protein G Recombinant

    Product # :

    PRO-402

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    • sds-page

    Description

    The Protein G is a single, non-glycosylated protein contains 200 amino acids having a molecular mass of 21.8kDa. The Protein-G migrates on SDS-PAGE around 32kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized white powder containing no additives.

    Purity

    >96% as determined by SDS-PAGE and RP-HPLC.

    sds-page

    Protein-G sds-page - Product image 1

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Recombinant Protein G although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Protein G should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      Reconstitution with deionized water or PBS.

    • Amino Acid Sequence

      LPKTDTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDAT KTFTVTEKPEVIDASELTPAVTTYKLVINGKTLKGETTTEAVDAATAEKVFK QYANDNGVDGEWTYDDATKTFTVTEKPEVIDASELTPAVTTYKLVINGKTL KGETTTKAVDAETAEKAFKQYANDNGVDGVWTYDDATKTFTVTE.

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

    Protein G
  • View Data Sheet

    Name :

    Ara h 1.0101

    Description:

    Allergen Ara h 1.0101 Recombinant

    Allergen Ara h 1, clone P41B, Allergen Ara h I, Allergen, Ara h 1.

    Product # :

    ALR-006

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    Description

    Recombinant Allergen Ara h 1.0101 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 63,484 Dalton. Ara h 1.0101 is expressed with a 9xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Ara h 1.0101 is supplied in 20mM HEPES buffer pH-8.0, 100mM Nacl and 6M Urea.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ara h 1 is a seed storage protein from Arachis hypogaea which causes an allergic reaction in human. Ara h 1 is found in 95% of peanut allergic patients from North America. Nevertheless, peanut-allergic patients of European populations have fewer sensitizations to Ara h 1.

    • Synonyms

      Allergen Ara h 1, clone P41B, Allergen Ara h I, Allergen, Ara h 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

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

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

    Ara H 10101
  • View Data Sheet

    Name :

    PhI p 12

    Description:

    Pollen Allergen Phl p 12 Recombinant

    Profilin-1, Allergen Phl p 11, Pollen allergen Phl p 12, Phl p 12, PRO1, PHLPXI.

    Product # :

    ALR-016

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    Description

    Recombinant PhI p 12 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 15,607 Dalton. PhI p 12 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    PhI p 12 is supplied in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phl p 12.0101 a profilin, is a minor grass pollen allergen which is involved in cytoskeleton mobility by interacting with actin filaments. It is well recognized that IgE binding can cause immune cross-reactivity with profilins of plant-derived foods and pollen profilin.

    • Synonyms

      Profilin-1, Allergen Phl p 11, Pollen allergen Phl p 12, Phl p 12, PRO1, PHLPXI.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

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

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

    Phi P 12
  • View Data Sheet

    Name :

    Gliadin Native

    Description:

    Gliadin Triticum Aestivum Grain Native

    Product # :

    PRO-2675

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    Description

    The native Gliadin Triticum Aestivum Grain is purified from wheat by protein chemical methods.

    Formulation

    Gliadin is supplied in 20mM HEPES buffer pH-7.4 and 6M Urea.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gliadin is a common substrate of transglutaminase, which generates neo-epitopes by deamidation of glutamine side chains. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgG and IgA-type human auto antibodies in sera of patients diagnosed with celiac disease.2. Immunodot analysis with positive/negative samples.

    • Applications

      Western blot with patient sample.

    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.

    Gliadin Protein
  • View Data Sheet

    Name :

    PCSK1N Human

    Description:

    Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor Human Recombinant

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

    Product # :

    PRO-1819

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Pcsk1N Human
  • View Data Sheet

    Name :

    Troponin C-I-T Human

    Description:

    Cardiac Troponin C-I-T Complex Human Recombinant

    Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.

    Product # :

    PRO-344

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    Description

    Recombinant Human Cardiac Troponin C-I-T complex produced in E.Coli is a single, non-glycosylated, polypeptide chain having the Molar ratio on cTnC to cTnI to cTnT of 1:1:1. Mw is approximately 90kDa.The Cardiac Troponin C-I-T complex is purified by proprietary chromatographic techniques

    Source

    Escherichia Coli.

    Formulation

    Human Cardiac Troponin C-I-T complex solution contains 500 mM NaCl, 20mM Tris-HCl, 4mM CaCl2, 4mM MgCl2and 60 mM B-mercaptoethanol, pH 7.5.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817, Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.

    • Physical Appearance

      Sterile Filtered colourless liquid formualtion.

    • Stability

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

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

    Troponin Ic Human
  • View Data Sheet

    Name :

    CCL13 Human, His

    Description:

    Monocyte Chemotactic Protein-4 Human Recombinant (CCL13), His-Tag

    CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.

    Product # :

    CHM-275

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    Description

    MCP4 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 96 amino acids (24-98) and having a molecular mass of 10.8 kDa. The MCP-4 is fused to 21 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The His Tag 0.25mg/ml MCP4 protein solution contains PBS pH-7.4, 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCL13 chemokine is part of the CC chemokine family (TARC). CCL13 protein induces chemotaxis in monocytes, eosinophils, T lymphocytes, and basophils by binding cell surface G-protein linked chemokine receptors such as CCR2, CCR3 and CCR5. CCL13 is induced by the inflammatory cytokines IL1 & TNFA.

    • Synonyms

      CKb10, MCP-4, NCC-1, NCC1, SCYA1, SCYL1, CK-beta-10, Small-inducible cytokine A13.

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQPDALNVPS TCCFTFSSKK ISLQRLKSYV ITTSRCPQKA VIFRTKLGKE ICADPKEKWV QNYMKHLGRK
      .AHTLKT

    • Background

      What is the molecular weight/Mw of CCL13 HUMAN, HIS Protein?
      CCL13 HUMAN, HIS Protein has a total Mw of 10.8kDa.

      What is the source or expression system of CCL13 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL13 HUMAN, HIS Protein?
      CCL13 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL13 HUMAN, HIS Protein?
      The biological functionality of CCL13 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL13 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MQPDALNVPS TCCFTFSSKK ISLQRLKSYV ITTSRCPQKA VIFRTKLGKE ICADPKEKWV QNYMKHLGRK
      .AHTLKT

      What applications can CCL13 HUMAN, HIS Protein be used in?
      CCL13 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL13 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL13 HUMAN, HIS 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.

    Mcp4 Human His
  • View Data Sheet

    Name :

    RPS27A Human, Biotin

    Description:

    Ubiquitin Biotinylated Human Recombinant

    Ubiquitin, Ribosomal Protein S27a, CEP80, UBA80, UBCEP1, UBCEP80, HUBCEP80, RPS27A.

    Product # :

    PRO-629

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    Description

    Recombinant Human RPS27A protein biotinylated with NHS-biotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 76 amino acids and having a molecular mass of 8.6 kDa.

    Source

    Escherichia Coli.

    Formulation

    The RPS27A is supplied in 1x PBS and 0.05% PBS.

    Purity

    RPS27A Protein biotinilation is determined by Western Blotting and ELISA analysis using streptavidin–HRP conjugated as a detection reagent. Free biotin is eliminated by dialysis against PBS. Protein concentration is determined by 280nm absorbance.

    More Info

    • Introduction

      Recombinant Human Ubiquitin having the accession number of P62988 was conjugated to Biotin. RPS27A is a small protein composed of 76 amino acids. RPS27A is found only in eukaryotic organisms among which shows strong sequence conservation. The RPS27A protein is present in all cell types, thus giving rise to its name.
      RPS27A is found either in free form or conjugated to proteins through a covalent bond between the glycine at the C-terminal end and the side chains of lysine.
      The connection of multiple copies of RPS27A targets the proteins for degradation by the 26S proteosome. RPS27A ligation is an ATP-dependent multi-step process. RPS27A is activated by the E1 enzyme. The attachment of RPS27A to the target protein is catalyzed by the E2 enzyme acting in concert with E3 which is involved in the recognition of the substrate protein.

    • Synonyms

      Ubiquitin, Ribosomal Protein S27a, CEP80, UBA80, UBCEP1, UBCEP80, HUBCEP80, RPS27A.

    • 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). Please prevent freeze-thaw cycles.

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

    RPS27A Human, Biotin
  • View Data Sheet

    Name :

    Collagen-I Goat

    Description:

    Goat Collagen-I

    Product # :

    PRO-2682

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    • More Info

    Description

    Goat Collagen-I is a natural protein purified from Goat tissues. Collagen-I is purified by proprietary chromatographic techniques.

    Source

    Goat tissues.

    Formulation

    Collagen-I was lyophilized without additives.

    Purity

    Greater than 90.0% as determined by SDS-PAGE 90.0%.

    More Info

    • Introduction

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

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Collagen-I although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-I should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to Add 0.5 M acetic acid, pH 2.5 to prepare a working stock solution not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Collagen I Goat
  • View Data Sheet

    Name :

    R-Spondin-1 Human

    Description:

    R-Spondin-1 Human Recombinant

    R-spondin-1, Cristin-3, mCristin-3, Roof plate-specific spondin-1, Rspo1, RSPO, R-spondin 1, R-spondin, Rspondin, CRISTIN3.

    Product # :

    PRO-2593

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    • More Info

    Description

    R-Spondin-1 Human Recombinant produced in CHO cells is a glycosylated monomer chain containing 243 amino acids and having a total molecular mass of 25.6kDa. RSPO1 is purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    The protein was lyophilized from a sterile (0.2µm) filtered solution containing PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as calculated by the Luciferase induction in HEK-293 STF cells in the presence of Murine Wnt-3a is 47.99ng/ml corresponding to a specific activity of 2.1 x 10^4 units/mg.

    More Info

    • Introduction

      R-Spondin-1 (Rspo1) is a part of the Rspondin family. Rspo1 plays a role as an activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Rspo1 induces the onset of crypt cell proliferation and increases intestinal epithelial healing effect. Rspo1 is negatively regulating the TGF-beta pathway.

    • Synonyms

      R-spondin-1, Cristin-3, mCristin-3, Roof plate-specific spondin-1, Rspo1, RSPO, R-spondin 1, R-spondin, Rspondin, CRISTIN3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized RSPO1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RSPO1 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized RSPO1in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SRGIKGKRQR RISAEGSQAC AKGCELCSEV NGCLKCSPKL FILLERNDIR QVGVCLPSCP PGYFDARNPD MNKCIKCKIE HCEACFSHNF CTKCKEGLYL HKGRCYPACP EGSSAANGTM ECSSPAQCEM SEWSPWGPCS KKQQLCGFRR GSEERTRRVL HAPVGDHAAC SDTKETRRCT VRRVPCPEGQ KRRKGGQGRR ENANRNLARK ESKEAGAGSR RRKGQQQQQQ QGTVGPLTSA GPA.

    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.

    R Spondin 1 Human
  • View Data Sheet

    Name :

    ADI1 Antibody

    Description:

    Acireductone Dioxygenase 1, Mouse Anti Human

    APL1, ARD, FLJ10913, HMFT1638, MTCBP-1, SIPL, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, Acireductone dioxygenase, Fe-ARD, Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1, Submergence-induced protein-like factor.

    Product # :

    ANT-466

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    • More Info

    Formulation

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

    More Info

    • Introduction

      Acireductone dioxygenase 1 (ADI1) is a part of the acireductone dioxygenase family of metal-binding enzymes, which are involved in methionine salvage. ADI1 regulates mRNA processing in the nucleus, and carries out different functions depending on its localization. Related pseudogenes have been defined on chromosomes 8 and 20. ADI1 down-regulates cell migration arbitrated by MMP14.

    • Synonyms

      APL1, ARD, FLJ10913, HMFT1638, MTCBP-1, SIPL, 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase, Acireductone dioxygenase, Fe-ARD, Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein 1, Submergence-induced protein-like factor.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human ADI1 mAb, clone PAT27E8A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human ADI1 protein 1-179 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and Kappa light chain.

    • Clone

      PAT27E8A.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1:5000. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

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

    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.

    Adi1 Antibody
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