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Search results

1000 results found for “serine peptidase inhibitor”

Name

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  • View Data Sheet

    Name :

    LL-37

    Description:

    LL-37

    LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.

    Product # :

    HOR-041

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    Description

    LL-37 Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 4493 Dalton and a Molecular formula of C205H340N60O53.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Synonyms

      LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LL-37 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LL-37 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 LL-37 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      H-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH.

    • Background

      LL-37, a prominent member of the human cathelicidin family, has emerged as a pivotal host defense peptide with diverse biological functions. This research paper aims to provide a comprehensive analysis of LL-37, elucidating its biochemical properties, antimicrobial activity, immunomodulatory effects, and potential therapeutic applications.

      LL-37, derived from the precursor protein hCAP18, plays a crucial role in innate immunity and host defense against microbial pathogens. Beyond its well-established antimicrobial properties, LL-37 exhibits various immunomodulatory effects, making it an intriguing target for therapeutic interventions (Lai & Gallo, 2009). This paper aims to delve into the complexities of LL-37, uncovering its multifaceted nature and potential clinical applications.

      LL-37 is a cationic peptide characterized by a helical structure that facilitates its interaction with microbial membranes. Its amphipathic nature enables it to penetrate microbial membranes, leading to disruption and subsequent cell death (Zaiou, 2007). Additionally, LL-37 can undergo proteolytic processing to release smaller bioactive fragments with distinct functions (Bowdish et al., 2005).

      LL-37's antimicrobial activity extends beyond direct microbial killing. It also exhibits immunomodulatory effects, stimulating the recruitment of immune cells and promoting the clearance of pathogens through phagocytosis (Scott et al., 2002). Furthermore, LL-37 can neutralize endotoxins, reducing inflammation caused by microbial products (Davidson et al., 2004).

      LL-37 possesses immunomodulatory properties that influence various immune cells, including neutrophils, macrophages, dendritic cells, and lymphocytes (Nagaoka et al., 2001). It can promote the differentiation and maturation of immune cells, modulate cytokine production, and contribute to wound healing and tissue repair (van Harten et al., 2018).

      The multifunctional nature of LL-37 renders it a promising candidate for various therapeutic applications. LL-37-based therapies are being explored in wound healing, infectious diseases, and immune-related disorders (Pena et al., 2014). Furthermore, LL-37 has shown potential as a vaccine adjuvant, enhancing the immune response to antigens (Howell et al., 2018).

      LL-37's diverse roles in immunity and host defense warrant further research to unravel its precise mechanisms of action and potential applications in clinical medicine. As we deepen our understanding of LL-37's complexities, its therapeutic potential continues to expand, offering exciting prospects for the future.

    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.

    Ll 37
  • View Data Sheet

    Name :

    SAA Equine

    Description:

    Serum Amyloid A (APO-SAA) Equine Recombinant

    Product # :

    CYT-1222

    Price :

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    Description

    SAA Equine produced in E.coli is a single, non-glycosylated polypeptide chain (1-110 a.a) containing 120 a.a and having a molecular mass of 13,580 Dalton. SAA s fused with a 10 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SAA was lyophilized from 0.01M HCl (pH 2.0).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SAA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serum Amyloid A (APO-SAA) 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 SAA in 0.01M HCl (pH 2.0) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Elevated SAA levels serve as sensitive markers for various inflammatory disorders, including infections, autoimmune diseases, and cancer. SAA assays, often utilizing recombinant SAA proteins, are invaluable in clinical diagnostics, aiding in disease monitoring and treatment evaluation. Moreover, the targeted modulation of SAA activities presents novel therapeutic strategies, offering potential interventions in conditions characterized by excessive inflammation.

      SAA Recombinant Protein, as a representative of the intricate SAA family, embodies the complexities of inflammation, immune regulation, and lipid metabolism. Its versatile roles in health and disease underscore its significance in biology and medicine. By unraveling the molecular intricacies of SAA, scientists pave the way for innovative diagnostic methods, therapeutic interventions, and a deeper understanding of the intricate interplay between inflammation and various physiological processes. This research not only illuminates the multifaceted nature of SAA but also holds the promise of transformative advancements in both clinical practice and scientific discovery.

    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.

    Saa Equine
  • View Data Sheet

    Name :

    NPPC Human

    Description:

    Natriuretic Peptide C Human Recombinant

    Natriuretic Peptide Precursor C, C-Type Natriuretic Peptide, CNP2, CNP.

    Product # :

    CYT-760

    Price :

    Quantity :

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    Description

    NPPC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 126 amino acids (24-126) and having a molecular mass of 13.2kDa.NPPC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      NPPC is proteolytically managed to create a secreted hormone of the natriuretic peptide family. NPPC is vasoactive and natriuretic and controls the evolution and differentiation of cartilaginous growth plate chondrocytes.

    • Synonyms

      Natriuretic Peptide Precursor C, C-Type Natriuretic Peptide, CNP2, CNP.

    • 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 MGSKPGAPPK VPRTPPAEEL AEPQAAGGGQ KKGDKAPGGG GANLKGDRSR LLRDLRVDTK SRAAWARLLQ EHPNARKYKG ANKKGLSKGC FGLKLDRIGS MSGLGC

    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.

    Nppc Human
  • View Data Sheet

    Name :

    OmpA S.Enteritidis

    Description:

    Salmonella Enteritidis Outer Membrane Protein-A Recombinant

    Outer Membrane Protein-A, OmpA.

    Product # :

    PRO-1918

    Price :

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    Description

    The Recombinant Salmonella Enteritidis Outer Membrane Protein A, E.Coli derived, 330 amino acids, contains the ompA immunodominant regions. The protein is fused to a His tag at C-terminal and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    PBS and 25MmM Arginine.

    Purity

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

    More Info

    • Introduction

      The OmpA protein is one of the main outer-membrane proteins of a large array of Gram-negative bacteria such as A.salmonicida, Shigella dysenteriae and E.coli.OmpA’s major physiological functions include maintenance of the structural integrity and morphology of the cells and porin activity, as well as a role in conjugation and bacteriophage binding.Achromogenic atypical Aeromonas salmonicida is the causative agent of goldfish ulcer disease.Virulence of this bacterium is associated with the production of a paracrystalline outer membrane A-layer protein.The species specific structural gene for the monomeric form of A-protein was cloned into a pET-3d plasmid in order to express and produce a recombinant form of the protein in E.coli BL21(DE3). The induced protein was isolated from inclusion bodies by a simple solubilization-renaturation procedure and purified by ion exchange chromatography on Q-Sepharose to over 95% pure monomeric protein.Recombinant A-protein was compared by biochemical, immunological and molecular methods with the A-protein isolated from atypical A.salmonicida bacterial cells by the glycine and the membrane extraction methods.

    • Synonyms

      Outer Membrane Protein-A, OmpA.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      OmpA S.Enteritidis Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Immunoassay. Outer membrane protein A (ompA) of S. Enteritidis is a protein directly exposing to outsides of this organism, In hens, the production of antibodies against outer membrane protein A (ompA) during the infection has been demonstrated by inoculating both the complete bacterium and expressed protein produced from ompA DNA vaccine. Vaccination by ompA protein to hens is a poteintail tool to control S. enteritidis contaminated eggs into market, and prevent human foodborne disease from eggs.

    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.

    Ompa Senteritidis
  • View Data Sheet

    Name :

    SAT1 Human

    Description:

    Spermidine/Spermine N1-Acetyltransferase 1 Human Recombinant

    Diamine acetyltransferase 1, Spermidine/spermine N(1)-acetyltransferase 1, Putrescine acetyltransferase, Polyamine N-acetyltransferase 1, SSAT-1, SSAT, SAT1, SAT, DC21, KFSD, KFSDX.

    Product # :

    ENZ-433

    Price :

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    Description

    SAT1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids (1-171 a.a.) and having a molecular mass of 22.1kDa.The SAT1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SAT1 solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SAT-1 is a member the acetyltransferase family, and is a rate-limiting enzyme in the catabolic pathway of polyamine metabolism. SAT1 catalyzes the acetylation of spermidine and spermine, and is involved in the regulation of the intracellular concentration of polyamines and their transport out of cells. Therefore, SAT-1’s role is essential in polyamine homoeostasis, given that acetylated products are either excreted from the cell or oxidized by acetylpolyamine oxidase. Increased SAT1 activity causes variety of other effects which include pancreatic cells death, obstruction of regenerative tissue growth, behavioral changes, keratosis follicularis spinulosa decalvans (KFSD), and hair loss.
      Defects in the SAT1 gene are linked to KFSD (keratosis follicularis spinulosa decalvans), which is a rare X-linked disorder affecting the skin and the eye. The KFSD affected men show thickening of the skin of the neck, ears, and extremities, particularly the palms and soles, loss of eyebrows, eyelashes and beard, thickening of the eyelids with blepharitis and ectropion, and corneal degeneration. Even though the majority of the affected families are compatible with an X-linked inheritance, KFSD are found to be clinically and genetically heterogeneous.

    • Synonyms

      Diamine acetyltransferase 1, Spermidine/spermine N(1)-acetyltransferase 1, Putrescine acetyltransferase, Polyamine N-acetyltransferase 1, SSAT-1, SSAT, SAT1, SAT, DC21, KFSD, KFSDX.

    • 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 MAKFVIRPAT AADCSDILRL IKELAKYEYM EEQVILTEKD LLEDGFGEHP FYHCLVAEVP KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMRC RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMATE E.

    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.

    Sat1 Human
  • View Data Sheet

    Name :

    QDPR Human

    Description:

    Quinoid Dihydropteridine Reductase Human Recombinant

    Dihydropteridine reductase, HDHPR, Quinoid dihydropteridine reductase, QDPR, DHPR, PKU2, SDR33C1.

    Product # :

    ENZ-163

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    Description

    QDPR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 267 amino acids (1-244 a.a.) and having a molecular mass of 28.2kDa.QDPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    QDPR protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      QDPR belongs to the short-chain dehydrogenases/reductase (SDR) family of enzymes. Operating as a homodimer, QDPR has an imperative role in the recycling of tetrahydrobiopterin (BH4), a vital cofactor for the hydroxylation of the aromatic amino acids (tryptophan, tyrosine and phenylalanine). More precisely, QDPR catalyzes the regeneration of BH4 from quinonoid dihydrobiopterin (qBH2), the product generated from the hydroxylation reactions. Mutations in the QDPR gene may lead to phenylketonuria II.

    • Synonyms

      Dihydropteridine reductase, HDHPR, Quinoid dihydropteridine reductase, QDPR, DHPR, PKU2, SDR33C1.

    • 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 MGSMAAAAAA GEARRVLVYG GRGALGSRCV QAFRARNWWV ASVDVVENEE ASASIIVKMT DSFTEQADQV TAEVGKLLGE EKVDAILCVA GGWAGGNAKS KSLFKNCDLM WKQSIWTSTI SSHLATKHLK EGGLLTLAGA KAALDGTPGM IGYGMAKGAV HQLCQSLAGK NSGMPPGAAA IAVLPVTLDT PMNRKSMPEA DFSSWTPLEF LVETFHDWIT GKNRPSSGSL IQVVTTEGRT ELTPAYF.

    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.

    Qdpr Human
  • View Data Sheet

    Name :

    ACY1 Antibody

    Description:

    AminoAcylase-1, Mouse Anti Human

    ACY1D, ACYLASE, ACY-1, EC 3.5.1.143.

    Product # :

    ANT-555

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    Formulation

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

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    • Introduction

      ACY1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to take part in the catabolism and salvage of acylated amino acids. Defects in ACY1 are the source of aminoacylase-1 deficiency (ACY1D). ACY1D results in a metabolic disorder manifesting with encephalopathy, unspecific psychomotor delay, psychomotor delay with atrophy of the vermis and syringomyelia, marked muscular hypotonia or normal clinical features. Epileptic seizures are a frequent feature.

    • Synonyms

      ACY1D, ACYLASE, ACY-1, EC 3.5.1.143.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human ACY1 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human ACY1 amino acids 1-408 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and ? light chain.

    • Clone

      PAT1E2AT.

    • Applications

      ACY1 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 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.

    • Purification Method

      ACY1 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.

    Acy1 Antibody
  • View Data Sheet

    Name :

    BIRC7 Human, (1-280 a.a.)

    Description:

    Baculoviral IAP Repeat-Containing 7 (1-280 a.a.) Human Recombinant

    Baculoviral IAP repeat-containing protein 7, KIAP, MLIAP, RNF50, ML-IAP, LIVIN, Kidney inhibitor of apoptosis protein, Melanoma inhibitor of apoptosis protein, RING finger protein 50, BIRC7.

    Product # :

    PRO-1042

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    Description

    BIRC7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (1-280 a.a.) and having a molecular mass of 33.4kDa.BIRC7 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BIRC7 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 40% glycerol, 300mM NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BIRC7 is a part of the inhibitor of apoptosis protein (IAP) family and contains a single copy of a baculovirus IAP repeat (BIR) as well as a RING-type zinc finger domain. The BIR domain is necessary for inhibitory activity & cooperates with caspases, while the RING finger domain sometimes increases anti-apoptotic activity but doesn’t inhibit apoptosis by itself. 2 transcript variants encoding diverse isoforms have been found for this gene. The 2 isoforms have dissimilar antiapoptotic characteristics, with isoform a protecting cells from apoptosis induced by staurosporine and isoform b defending cells from apoptosis induced by etoposide.
      BIRC7 has direct contact with several caspases together with caspase-3, caspase-7, & caspase –9. BIRC7 inhibits the activation of caspase-9 induced by Apaf-1, cytochrome c, and dATP.

    • Synonyms

      Baculoviral IAP repeat-containing protein 7, KIAP, MLIAP, RNF50, ML-IAP, LIVIN, Kidney inhibitor of apoptosis protein, Melanoma inhibitor of apoptosis protein, RING finger protein 50, BIRC7.

    • 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 MGSHMGPKDS AKCLHRGPQP SHWAAGDGPT QERCGPRSLG SPVLGLDTCR AWDHVDGQIL GQLRPLTEEE EEEGAGATLS RGPAFPGMGS EELRLASFYD WPLTAEVPPE LLAAAGFFHT GHQDKVRCFF CYGGLQSWKR GDDPWTEHAK WFPSCQFLLR SKGRDFVHSV QETHSQLLGS WDPWEEPEDA APVAPSVPAS GYPELPTPRR EVQSESAQEP GARDVEAQLR RLQEERTCKV CLDRAVSIVF VPCGHLVCAE CAPGLQLCPI CRAPVRSRVR TFLS.

    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.

    Birc7 Human 1 280 Aa
  • View Data Sheet

    Name :

    Clusterin Antibody

    Description:

    Clusterin, Mouse Anti Human

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.

    Product # :

    ANT-314

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    Formulation

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

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    • 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 ? and ? 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 ? -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, b

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Complement-associated protein SP-40,40, Complement cytolysis inhibitor, NA1/NA2, Apolipoprotein J, Apo-J, Testosterone-repressed prostate message 2, TRPM-2.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Immunogen

      Anti-human Clusterin mAb, is derived from hybridization of mouse SP2/O myeloma cells with spleen cells from BALB/c mice immunized with Recombinant human Clusterin amino acids 1-333 purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      P1A11AT.

    • Applications

      Clusterin antibody has been tested by ELISA, Western blot, ICC/IF, IHC and FACS analysis 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

      Clusterin antibody was purified from mouse ascitic fluids by protein-G 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.

    Clusterin Antibody
  • View Data Sheet

    Name :

    AKR7A3, Human

    Description:

    Aldo-Keto Reductase Family 7 Member A3 Human Recombinant

    AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.

    Product # :

    ENZ-1129

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    Description

    AKR7A3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-331) and having a molecular mass of 37.7 kDa.AKR7A3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR7A3 solution (1mg/ml) contains 10% Glycerol and 20mM Tris-HCl buffer (pH 8.5).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 800pmol/min/ug. It is defined by the amount of enzyme that catalyzes the reduction 1.0pmole of 1,2-Naphthoquinone presence of NADPH per minute at pH 7.0 at 25˚C.

    More Info

    • Introduction

      Aldo-Keto Reductase Family 7 Member A3 or AKR7A3, is an enzyme, it is part of the detoxification of aldehydes and ketones process. AKR7A3 diminishes the dialdehyde protein-binding form of aflatoxin B1 to the non-binding AFB1 dialcohol. The enzyme takes partin protection of liver from toxic and carcinogenic effects of AFB1, a potent hepatocarcinogen.

    • Synonyms

      AFAR2, Aflatoxin B1 aldehyde reductase member 3, AFB1 aldehyde reductase 2, AFB1-AR 2, AKR7A3.

    • 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

      MSRQLSRARP ATVLGAMEMG RRMDAPTSAA VTRAFLERGH TEIDTAFVYS EGQSETILGG LGLRLGGSDC RVKIDTKAIP LFGNSLKPDS LRFQLETSLK RLQCPRVDLF YLHMPDHSTP VEETLRACHQ LHQEGKFVEL GLSNYAAWEV AEICTLCKSN GWILPTVYQG MYNAITRQVE TELFPCLRHF GLRFYAFNPL AGGLLTGKYK YEDKDGKQPV GRFFGNTWAE MYRNRYWKEH HFEGIALVEK ALQAAYGASA PSMTSATLRW MYHHSQLQGA HGDAVILGMS SLEQLEQNLA AAEEGPLEPA VVDAFNQAWH LVAHECPNYF R

    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.

    Akr7A3 Enzyme
  • View Data Sheet

    Name :

    TIMP4 Human

    Description:

    Tissue Inhibitor of Metalloprotease 4 Human Recombinant

    TIMP Metallopeptidase Inhibitor 4, Tissue Inhibitor Of Metalloproteinases 4, Tissue Inhibitor Of Metalloproteinase 4, TIMP-4, Metalloproteinase Inhibitor 4.

    Product # :

    ENZ-976

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    Description

    TIMP4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 204 amino acids (30-224 a.a.) and having a molecular mass of 23.5kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). TIMP4 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    TIMP4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Metalloproteinase inhibitor 4 (TIMP4) is a member of a family of secreted proteins which regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases. The four known members of this family are TIMP1, 2, 3 and 4. TIMP4 is produced by various tissues, particularly the brain, heart, ovary and skeletal muscle. Limited studies have shown that the TIMP4 protein has a tumor suppressive effect against Wilm92s tumor, exhibiting a negative correlation with glioma malignancy and is found in breast carcinoma cells.

    • Synonyms

      TIMP Metallopeptidase Inhibitor 4, Tissue Inhibitor Of Metalloproteinases 4, Tissue Inhibitor Of Metalloproteinase 4, TIMP-4, Metalloproteinase Inhibitor 4.

    • 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

      ADPCSCAPAH PQQHICHSAL VIRAKISSEK VVPASADPAD TEKMLRYEIK QIKMFKGFEK VKDVQYIYTP FDSSLCGVKL EANSQKQYLL TGQVLSDGKV FIHLCNYIEP WEDLSLVQRE SLNHHYHLNC GCQITTCYTV PCTISAPNEC LWTDWLLERK LYGYQAQHYV CMKHVDGTCS WYRGHLPLRK EFVDIVQPHH HHHH.

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

    Timp4 Human
  • View Data Sheet

    Name :

    Buserelin

    Description:

    Buserelin

    Product # :

    HOR-255

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    Description

    Buserelin contains 9 amino acids Glu-His-Trp-Ser-Tyr-D-Ser(tBu)-Leu-Arg-Pro-NHEt and having a molecular weight of 1239.44 Dalton.

    Formulation

    The Buserelin peptide was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Buserelin belongs to the group of gonadotrophin releasing hormone (gonadorelin) analogues (LHRH agonist). It acts on the pituitary gland which controls the amount of many different types of hormones (chemical messengers). It alters the amount of hormones, particularly the oestrogens androgens. This alteration of hormone levels can be exploited to treat cancers of the prostate gland, which are stimulated to grow by testosterone. Buserelin lowers the levels of testosterone, which starves the tumour of testosterone and causes it to shrink.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    Buserelin
  • View Data Sheet

    Name :

    CEA Human

    Description:

    Carcinoembryonic Antigen Human Recombinant

    CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    Product # :

    PRO-287

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    Description

    CEA Human Recombinant is glycosylated with N-linked sugars and produced using baculovirus vectors in insect cells. CEA is a well-known tumor marker corresponding to the full length human CEA which is approximately 120,000 Dalton.

    Source

    Baculovirus Insect Cells.

    Formulation

    The sterile protein solution contains 10mM NaH2PO4, pH 7 and 150mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carcinoembryonic antigen (CEA) is a glycoprotein present in fetal digestive-tract tissues; it’s involved in cell adhesion. The production of CEA stops before birth. CEA is called tumor marker since its elevated levels are found in the serum from individuals with colorectal, gastric, pancreatic, lung and breast carcinomas and in heavy smokers.
      There are also benign conditions that elevate CEA levels such as smoking, infection, inflammatory bowel disease, pancreatitis, cirrhosis of the liver, and some benign tumors (in the equivalent organs which have cancers with elevated CEA). Typically, higher levels of CEA are found in men, smokers, and older individuals.
      The presence of CEA assists in screening, in evaluating recurrent or disseminated disease, and in determining the success of surgical removal of malignant tumors.
      CEA levels can be used as indicators of treatment success. The normal values range from 0.0 to 2.5 ng/ml of serum (from blood), in non-smokers, a greater amount than that may be suggestive of cancer. Levels above 20 ng/ml before treatment are associated with cancer which has already metastasized. Benign conditions do not usually cause a CEA increase over 10 ng/ml.
      The high levels of CEA should return to normal after successful therapy, however if during follow up there’s an elevation in CEA levels it indicates a recurrence of tumor.
      Carcinoembryonic antigen family belongs to the immunoglobulin superfamily; it consists of 29 genes, 18 of which are normally expressed.

    • Synonyms

      CEACAM5, Meconium Antigen 100, Carcinoembryonic Antigen, CD66e Antigen, CD66e, Carcinoembryonic Antigen, CEA, oncofetal antigen.

    • Physical Appearance

      Sterile Filtered colourless solution.

    • Stability

      CEA should be stored at 2-8°C.Avoid freezing.

    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.

    Carcinoembryonic Antigen
  • View Data Sheet

    Name :

    MMP 13 Human

    Description:

    Matrix Metalloproteinase-13 Human Recombinant

    CLG3, MANDP1, Matrix metalloproteinase-13, MMP-13, MMP13.

    Product # :

    ENZ-317

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    Description

    MMP-13 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 391 amino acids (104-471 a.a.) and having a molecular mass of 44.7 kDa. MMP-13 is fused to a 23 amino acid His Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MMP-13 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Matrix Metalloproteinase-13 (MMP-13) is an enzyme that is a member of the MMP extracellular protease family. Extracellular protease enzymes, by virtue of their broad substrate specificities1, play a role in both normal and disease states of tissue proliferation. Among the targets of MMP-13 are collagen, gelatin, entactin, pro-TNF-a, and chemokine SDF-11-4.
      MMP-13 is found in its latent form as a 52-56 kDa glycosylated proenzyme. Upon cleavage the 22-46 kDa5 MMP-1 becomes active in extracellular matrix remodeling.
      Because of the prominent role that MMP-1 plays in cell migration and metastasis, it is an important target for inhibition screening.

    • Synonyms

      CLG3, MANDP1, Matrix metalloproteinase-13, MMP-13, MMP13.

    • 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 MGSYNVFPRT LKWSKMNLTY RIVNYTPDMT HSEVEKAFKK AFKVWSDVTP LNFTRLHDGI ADIMISFGIK EHGDFYPFDG PSGLLAHAFP PGPNYGGDAH FDDDETWTSS SKGYNLFLVA AHEFGHSLGL DHSKDPGALM FPIYTYTGKS HFMLPDDDVQ GIQSLYGPGD EDPNPKHPKT PDKCDPSLSL DAITSLRGET MIFKDRFFWR LHPQQVDAEL FLTKSFWPEL PNRIDAAYEH PSHDLIFIFR GRKFWALNGY DILEGYPKKI SELGLPKEVK KISAAVHFED TGKTLLFSGN QVWRYDDTNH IMDKDYPRLI EEDFPGIGDK VDAVYEKNGY IYFFNGPIQF EYSIWSNRIV RVMPANSILW C.

    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.

    Mmp13 Human
  • View Data Sheet

    Name :

    CDKN1A Human (20-149)

    Description:

    Cyclin-Dependent Kinase Inhibitor 1A (20-149 a.a.) Human Recombinant

    Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.

    Product # :

    PKA-137

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    Description

    The CDKN1A Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The CDKN1A His-Tagged Fusion Protein, produced in E. coli, is a 20kDa protein containing 130 amino acid residues of the CDKN1A Human, 20-149 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized CDKN1A at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

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

    • Amino Acid Sequence

      LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLEGDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLVPRSGEQAEGS PGGPGDSQGR KRRQTSMTDF

    • Background

      CDKN1A gene in humans plays an important role in maintaining genomic stability which is critical to cancer prevention and proper function of regular cellular processes. CDKN1A plays a main role in the cellular response to DNA mutation. CDKN1A overexpression causes cell cycle to stop. CDKN1A, along with CDK2 complexes aids to prevent kinase activity and inhibits progression through G1/S. CDKN1A can additionally increase assembly and activity in complexes of CDK4 or CDK6 and cyclin D.

    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.

    Cdkn1A Protein
  • View Data Sheet

    Name :

    GST Monoclonal antibody

    Description:

    Glutathione-S-Transferase, Mouse antibody

    Product # :

    ANT-219

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    Description

    Monoclonal antibodies are produced by immunizing mouse with GST protein.

    Formulation

    1×PBS & 50% glycerol.

    More Info

    • Introduction

      GST family of enzymes comprises a long list of cytosolic, mitochondrial, and microsomal proteins that are 45-55 kDa (dimer form) size and are capable of multiple reactions with a multitude of substrates, both endogenous and xenobiotic. GST catalyses the conjugation of reduced glutathione meaning the sulfhydryl group, to electrophilic centers on a wide variety of substrates. This activity is useful in the detoxification of endogenous compounds such as peroxidised lipids, as well as the metabolism of xenobiotics. GST binds toxins and function as transport protein. Glutathione S-transferase is used to create the so-called 'GST gene fusion system'. The GST is used to purify and detect proteins of interest. In a GST gene fusion system, the GST sequence is incorporated into an expression vector alongside the gene sequence encoding the protein of interest. Induction of protein expression from the vector's multiple cloning sites results in expression of a fusion protein - the protein of interest fused to the GST protein. This GST-fusion protein can then be purified from cells via its high affinity for glutathione. Fusion proteins offer an important biological assay for direct protein-to-protein interactions. The GST tag has the size of 220 amino acids, which, compared to other tags like the myc- or the FLAG-tag, is quite big. It is fused to the N-terminus of a protein. However, many commercially-available sources of GST-tagged plasmids include a thrombin domain for cleavage of the GST tag during protein purification. A GST-tag is often used to separate and purify proteins that contain the GST-fusion. GST-fusion proteins can be produced in Escherichia coli, as recombinant proteins.

    • Ig Subclass

      Mouse IgG2b.

    • Clone

      PGSTSHG.

    • Applications

      Western Blot, Immunoprecipitation.

    • Titer

      Western Blotting: 1μg/ml.

    • Type

      Mouse Antibody Monoclonal.

    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.

    Gst Igg2B Antibody
  • View Data Sheet

    Name :

    Tirzepatide

    Description:

    Tirzepatide

    Product # :

    HOR-057

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    Description

    Tirzepatide is a synthetic single, non-glycosylated polypeptide chain containing 39 amino acids, having a molecular mass of 4813 Dalton and a Molecular formula of C187H291N45O59.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      His-Ala-Glu-Gly-Thr-Phe-Thr-Ser-Asp-Tyr-Ser-Ile-Aib-Leu-Asp-Lys-Ile-Ala-Gln-Lys (Eicosanedioyl-isoGlu-PEG2-PEG2)-Ala-Phe-Val-Gln-Trp-Leu-Ile-Ala-Gly-Gly-Pro-Ser-Ser-Gly-Ala-Pro-Pro-Pro-Ser-NH2.

    • Background

      Tirzepatide is a first-in-class dual glucose-dependent insulinotropic polypeptide and glucagon-like peptide-1 receptor agonist. Recent development suggests Tirzepatide as organ protection and systemic metabolic health while at first, it was only approved for Type 2 Diabetes and Chronic Weight Management. Preclinical data also indicates a promising future in neuroprotection and most likely to expand its clinical utility into neurodegenerative pathologies.

    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.

    Tirzepatide
  • View Data Sheet

    Name :

    PTRH2 Human

    Description:

    Peptidyl-tRNA Hydrolase 2 Human Recombinant

    Peptidyl-tRNA hydrolase 2, mitochondrial, PTH 2, Bcl-2 inhibitor of transcription 1, PTRH2, BIT1, PTH2, CGI-147, FLJ32471, PTRH2.

    Product # :

    ENZ-045

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    Description

    PTRH2 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 137 amino acids (64-179 a.a.) and having a molecular mass of 14.9kDa. The PTRH2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PTRH2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Peptidyl-tRNA hydrolase 2 (PTRH2) is a mitochondrial protein. PTRH2 is released during apoptosis from the mitochondria to the cytoplasm. When in the cytoplasm, PTRH2 regulates the function of 2 transcriptional regulators, TLE5 and TLE1, thus promoting caspase-independent cell death. Natural substrates for PTRH2 may be petidyl-tRNAs which drop off the ribosome during protein synthesis.

    • Synonyms

      Peptidyl-tRNA hydrolase 2, mitochondrial, PTH 2, Bcl-2 inhibitor of transcription 1, PTRH2, BIT1, PTH2, CGI-147, FLJ32471, PTRH2.

    • 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 MEYKMILVVR NDLKMGKGKV AAQCSHAAVS AYKQIQRRNP EMLKQWEYCG QPKVVVKAPD EETLIALLAH AKMLGLTVSL IQDAGRTQIA PGSQTVLGIG PGPADLIDKV TGHLKLY.

    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.

    Ptrh2 Human
  • View Data Sheet

    Name :

    MMP 8 Human, His

    Description:

    Matrix Metalloproteinase-8 Human Recombinant, His Tag

    CLG1, HNC, MMP-8, PMNL-CL, Neutrophil collagenase, Matrix metalloproteinase-8, MMP-8, PMNL collagenase.

    Product # :

    ENZ-766

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    Description

    MMP 8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (101-467a.a) and having a molecular mass of 44.3kDa. MMP 8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MMP 8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Full-length recombinant human neutrophil pro-collagenase (MMP-8), latent form.
      Matrix metalloproteinase 8 (MMP-8), or neutrophil collagenase, degrades interstitial collagens, acting preferentially on collagen type I.
      Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
      MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes.

    • Synonyms

      CLG1, HNC, MMP-8, PMNL-CL, Neutrophil collagenase, Matrix metalloproteinase-8, MMP-8, PMNL collagenase.

    • 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 MGSLTPGNPK WERTNLTYRI RNYTPQLSEA EVERAIKDAF ELWSVASPLI FTRISQGEAD INIAFYQRDH GDNSPFDGPN GILAHAFQPG QGIGGDAHFD AEETWTNTSA NYNLFLVAAH EFGHSLGLAH SSDPGALMYP NYAFRETSNY SLPQDDIDGI QAIYGLSSNP IQPTGPSTPK PCDPSLTFDA ITTLRGEILF FKDRYFWRRH PQLQRVEMNF ISLFWPSLPT GIQAAYEDFD RDLIFLFKGN QYWALSGYDI LQGYPKDISN YGFPSSVQAI DAAVFYRSKT YFFVNDQFWR YDNQRQFMEP GYPKSISGAF PGIESKVDAV FQQEHFFHVF SGPRYYAFDL IAQRVTRVAR GNKWLNCRYG.

    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.

    Mmp 8 Human His
  • View Data Sheet

    Name :

    SURA E.Coli

    Description:

    Chaperone SURA E.Coli Recombinant

    Rotamase surA, Survival protein A.

    Product # :

    ENZ-257

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    Description

    SURA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 429 amino acids (21-428 a.a.) and having a molecular weight of 47.3kDa. The SURA is fused to 20 a.a His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SURA 1mg/ml protein solution contains 20mM Tris-HCl, pH-8, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 450 nmoles/min/ug, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

      SURA is a PPIase enzyme and chaperone of Escherichia coli and other Gram-negative bacteria. SURA is a key player in the biogenesis of beta-barrel outer membrane proteins and is involved in cell envelope homeostasis and cell envelope functions. SURA is necessary for the survival of E.coli in stationary phase and needed for pilus biogenesis.

    • Synonyms

      Rotamase surA, Survival protein A.

    • 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 MAPQVVDKVA AVVNNGVVLE SDVDGLMQSV KLNAAQARQQ LPDDATLRHQ IMERLIMDQI ILQMGQKMGV KISDEQLDQA IANIAKQNNM TLDQMRSRLA YDGLNYNTYR NQIRKEMIIS EVRNNEVRRR ITILPQEVES LAQQVGNQND ASTELNLSHI LIPLPENPTS DQVNEAESQA RAIVDQARNG ADFGKLAIAH SADQQALNGG QMGWGRIQEL PGIFAQALST AKKGDIVGPI RSGVGFHILK VNDLRGESKN ISVTEVHARH ILLKPSPIMT DEQARVKLEQ IAADIKSGKT TFAAAAKEFS QDPGSANQGG DLGWATPDIF DPAFRDALTR LNKGQMSAPV HSSFGWHLIE LLDTRNVDKT DAAQKDRAYR MLMNRKFSEE AASWMQEQRA SAYVKILSN.

    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.

    Sura
  • View Data Sheet

    Name :

    HADHB Human

    Description:

    2-Enoyl-Coenzyme A (CoA) Hydratase, Beta Human Recombinant

    Hydroxyacyl-CoA Dehydrogenase/3-Ketoacyl-CoA Thiolase/Enoyl-CoA Hydratase (Trifunctional Protein) Beta Subunit, Hydroxyacyl-Coenzyme A Dehydrogenase/3-Ketoacyl-Coenzyme A Thiolase/Enoyl-Coenzyme A Hydratase (Trifunctional Protein) Beta Subunit, TP-BETA, 3-Ketoacyl-Coenzyme A (CoA) Thiolase Of Mitochondrial Trifunctional Protein Beta Subunit, 2-Enoyl-Coenzyme A (CoA) Hydratase Beta Subunit, Trifunctional Enzyme Subunit Beta Mitochondrial, Mitochondrial Trifunctional Protein, Acetyl-CoA Acyltransferase, Beta-Ketothiolase, Beta Subunit, EC 2.3.1.16, EC 2.3.1, MSTP029, ECHB, MTPB.

    Product # :

    ENZ-845

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    Description

    HADHB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 464 amino acids (34-474 a.a) and having a molecular mass of 49.9kDa. HADHB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HADHB protein solution (0. 5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      2-Enoyl-Coenzyme A (CoA) Hydratase, Beta (HADHB) is the beta subunit of the mitochondrial trifunctional protein, that catalyzes the last 3 phases of mitochondrial beta-oxidation of long chain fatty acids. HADHB binds RNA and reduces the stability of various mRNAs. Mutations in HADHB cause trifunctional protein deficiency.

    • Synonyms

      Hydroxyacyl-CoA Dehydrogenase/3-Ketoacyl-CoA Thiolase/Enoyl-CoA Hydratase (Trifunctional Protein) Beta Subunit, Hydroxyacyl-Coenzyme A Dehydrogenase/3-Ketoacyl-Coenzyme A Thiolase/Enoyl-Coenzyme A Hydratase (Trifunctional Protein) Beta Subunit, TP-BETA, 3-Ketoacyl-Coenzyme A (CoA) Thiolase Of Mitochondrial Trifunctional Protein Beta Subunit, 2-Enoyl-Coenzyme A (CoA) Hydratase Beta Subunit, Trifunctional Enzyme Subunit Beta Mitochondrial, Mitochondrial Trifunctional Protein, Acetyl-CoA Acyltransferase, Beta-Ketothiolase, Beta Subunit, EC 2.3.1.16, EC 2.3.1, MSTP029, ECHB, MTPB.

    • 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 MGSAAPAVQT KTKKTLAKPN IRNVVVVDGV RTPFLLSGTS YKDLMPHDLA RAALTGLLHR TSVPKEVVDY IIFGTVIQEV KTSNVAREAA LGAGFSDKTP AHTVTMACIS ANQAMTTGVG LIASGQCDVI VAGGVELMSD VPIRHSRKMR KLMLDLNKAK SMGQRLSLIS KFRFNFLAPE LPAVSEFSTS ETMGHSADRL AAAFAVSRLE QDEYALRSHS LAKKAQDEGL LSDVVPFKVP GKDTVTKDNG IRPSSLEQMA KLKPAFIKPY GTVTAANSSF LTDGASAMLI MAEEKALAMG YKPKAYLRDF MYVSQDPKDQ LLLGPTYATP KVLEKAGLTM NDIDAFEFHE AFSGQILANF KAMDSDWFAE NYMGRKTKVG LPPLEKFNNW GGSLSLGHPF GATGCRLVMA AANRLRKEGG QYGLVAACAA GGQGHAMIVE AYPK.

    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.

    Hadhb Human
  • View Data Sheet

    Name :

    Resistin Human (64-110)

    Description:

    Resistin (64-110) Human Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.

    Product # :

    CYT-1232

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    Description

    The Resistin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Resistin His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 47 amino acid residues of the Resistin Human, 64-110 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Background

      Human resistin is an adipokine primarily secreted by adipose tissue, mainly in response to obesity and inflammatory conditions.

      Resistin Function

      Resistin takes part in insulin resistance, which can be the cause of the development of type 2 diabetes. Resistin can also affect glucose metabolism and insulin signalling.

      Regulation

      Levels of resistin are influenced by factors such as inflammation, obesity and certain hormones. It tends to increase in conditions associated with obesity and metabolic syndrome.

      Clinical Relevance

      Elevated levels of resistin have been associated with obesity-related conditions, cardiovascular diseases, and metabolic disorders. Resisting is considered as a potential biomarker for these conditions.

      Resistin Mechanism

      Resistin promotes insulin resistance through different pathways such as the modulation of inflammatory processes and the inhibition of insulin signaling in target tissues like liver and muscle.

      Research

      Ongoing studies are exploring resistin’s role in metabolic regulation, the exact mechanisms of action of resistin and its potential as a therapeutic target for treating metabolic diseases.

      Overall, resistin is a critical factor in metabolic health, mainly in the context of diabetes and obesity.

    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.

    Resistin Human Protein
  • View Data Sheet

    Name :

    CSNK2A1 Human

    Description:

    Casein Kinase 2 alpha 1 Human Recombinant

    Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.

    Product # :

    PKA-208

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    • More Info

    Description

    Casein Kinase 2 alpha 1 Human Recombinant is a non-glycosylated polypeptide having a molecular mass of 45.1 kDa. Casein Kinase 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CSNK2A1 is supplied in 25mM Tris-HCl, 500mM NaCl, 1mM DTT, 500μm PMSF, 50% glycerol, pH 8.5.

    Purity

    Greater than 99% as determined by SDS-PAGE.

    More Info

    • Introduction

      The Casein kinase 2 (EC2.7.11.1) is a serine/threonine-selective protein kinasethat is a tetramer of two alpha subunits and two beta subunits. The alpha subunits have the catalytic kinase domain. Casein kinase 2 has been implicated in cell cyclecontrol, DNA repair, regulation of the circadian rhythmand other cellular processes. Casein kinase 2 activity has been reported to be activated following Wnt signaling pathwayactivation. A Pertussis toxin-sensitive G proteinand Disheveled appear to be an intermediary between Wnt-mediated activation of the Frizzled receptor and activation of casein kinase 2.
      Mice that lack casein kinase 2 alpha prime have a defect in the morphology of developing sperm.

    • Synonyms

      Casein kinase II subunit alpha, EC 2.7.11.1, CK II, CK2A1, CKII alpha, CSNK2A1, PKCK2, CSK21.

    • 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.

    • Unit Definition

      No protease activity detectable, specific activity > 1.320 U/mg (1U = 1µmol/min at 37 degree C) using the synthetic peptide RRRDDDSDDD.

    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.

    Csnk2A1 Human
  • View Data Sheet

    Name :

    Resistin Human, Antagonist

    Description:

    Resistin Antagonist Human Recombinant

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-1255

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    • More Info

    Description

    Resistin Human antagonist is a monomeric C7A mutant that does not form covalent dimers. Resistin Human antagonist is purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    Resistin was lyophilized from a concentrated (1mg/ml) solution with 0.03% NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Analysis by Gel Filtration.

    (b) Analysis by SDS-PAGE.

    (c) Analysis by RP-HPLC.

    Biological Activity

    The biological activity was evidenced by resistin antagonist activity to inhibit resistin-induced Akt phosphorylation in two cell lines. It also reduced the weight (mainly the visceral fat) and normalized GTT and ITT inHFD-fed mice.

    More Info

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Resistin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Resistin Mouse 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 Resistin in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first seven N-terminal amino acids was determined and was found to be Ala-Ser-Ser-Lys-Thr-Leu-Ala.

    • Background

      Resistin, also known as adipose tissue-specific secretory factor (ADSF) is a cysteine-rich peptide derived from adipose tissue. Resistin takes part in the inflammatory response, glucose metabolism, and angiogenesis. Resistin blocks insulin stimulated uptake of glucose by adipocytes and promote glucose release by hepatocytes. As such,Resistin considered to participate in diet‑induced insulin-sensitivity. Resistin causes high levels of low-density lipoprotein (LDL), increasing the risk of heart disease.

    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.

    Resistin Antagonist
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