Search results
1000 results found for “Paraoxonase”
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Name :
SPA-Cys HisDescription:
Staphylococcal Protein-A Cys Recombinant, His Tag
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-1923Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SPA-Cys His Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain with 6×His-tag and a Cys on C-terminus. SPA-Cys His is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 307 amino acids and having a molecular mass of 34.8kDa containing little or no carbohydrate. Cell wall binding region, cell membrane binding region and albumin binding region were removed to ensure the highest specific IgG binding.
Source
Escherichia Coli.
Formulation
SPA protein was lyophilized with no additives.
Purity
Greater than 96.0% as determined by: (a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
More Info
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Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA 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.
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Solubility
It is recommended to reconstitute the lyophilized SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MNAAQHDEAQ QNAFYQVLNM PNLNADQRNG FIQSLKDDPS QSANVLGEAQ KLNDSQAPKA DAQQNNFNKD QQSAFYEILN MPNLNEAQRN GFIQSLKDDP SQSTNVLGEA KKLNESQAPK ADNNFNKEQQ NAFYEILNMP NLNEEQRNGF IQSLKDDPSQ SANLLSEAKK LNESQAPKAD NKFNKEQQNA FYEILHLPNL NEEQRNGFIQ SLKDDPSQSA NLLAEAKKLN DAQAPKADNK FNKEQQNAFY EILHLPNLTE EQRNGFIQSL KDDPSVSKEI LAEAKKLNDA QAPKEEDSLE HHHHHHC
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.
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Name :
Anthrax PA AntibodyDescription:
Anthrax PA Polyclonal Antibody
Product # :
ANT-182Price :
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Shipped with Ice Packs
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Formulation
200µl PBS containing 0.05% BSA and 0.05% sodium azide.
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Introduction
Anthrax PA (Protective Antigen) and Anthrax LF (Lethal Factor), along with Anthrax EF (Edema Factor), are toxins produced by Bacillus anthracis. All three of the proteins must be present for toxicity to occur. It begins with the binding of PA to its cell-surface receptor, ATR (Anthrax Toxin Receptor), at which point PA is cleaved and the resulting 63 kD carboxyl-terminal fragment binds to LF and EF. LF is a protease that is known to cleave members of the mitogen-activated protein kinase kinase (MAPKK) family(2).
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Stability
Store at 4°C, stable for 6 months. For long-term storage, store at -20°C.
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Immunogen
Anthrax PA Antibody was developed by immunizing rabbits with synthetic peptides corresponding to amino acids 240-254 of the Anthrax PA protein (~83 kD). Anthrax PA Antibody is cleaved from the 83 kDa form to the 63 kDa form at amino acids 164-167. Thus the Anthrax PA antibody (made against amino acids 250-250) should recognize both the 83 kDa and 63 kDa PA forms, but not the 20 kDa cleavage fragment.
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Applications
This polyclonal antibody can be used for detection of Anthrax PA protein in western blot, 1:1000.
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Isotype
Rabbit Ig.
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Type
Rabbit Anti Human Polyclonal Antibody.
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.
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Name :
RNASE3 Human, Sf9Description:
Ribonuclease 3 Human Recombinant, Sf9
ECP, RNS3, Ribonuclease 3, Eosinophil cationic protein, RNASE3, RNASE3.
Product # :
ENZ-1024Price :
Quantity :
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Description
RNASE3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 142 amino acids (28-160 a.a.) and having a molecular mass of 16.6kDa (Migrates at 18-28kDa on SDS-PAGE under reducing conditions).RNASE3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
RNASE3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Ribonuclease 3 (RNASE3) is cytotoxin and helminthotoxin with low-efficiency ribonuclease activity. RNASE3 possesses a broad diversity of biological activities. RNASE3 protein has shown antibacterial activity such as cytoplasmic membrane depolarization of preferentially Gram-negative and Gram-positive strains and promotes E. coli outer membrane detachment, alteration of the overall cell shape and partial loss of cell content.
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Synonyms
ECP, RNS3, Ribonuclease 3, Eosinophil cationic protein, RNASE3, RNASE3.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
ADPRPPQFTR AQWFAIQHIS LNPPRCTIAM RAINNYRWRC KNQNTFLRTT FANVVNVCGN QSIRCPHNRT LNNCHRSRFR VPLLHCDLIN PGAQNISNCR YADRPGRRFY VVACDNRDPR DSPRYPVVPV HLDTTIHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CRP Paired AntibodyDescription:
Anti Human C-Reactive Protein Paired Antibody Mouse
Product # :
ANT-783Price :
Quantity :
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Shipped with Ice Packs
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Description
CRP Paired monoclonal antibodies are used to develop rapid test for CRP rapid test. Please note that when ordering for example: 100µg paired antibody, you receive 50µg from each antibody (100µg in total).
Formulation
* CRP conjugation antibody in PBS, NaCl and 0.095% NaN3.
* CRP coating antibody in PBS, NaCl and 0.095% NaN3.
Purity
Greater than 95%.
More Info
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Physical Appearance
2 vials of sterile Filtered clear colorless solution.
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Stability
For periods up to 1 month CRP Paired Antibody should be stored at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Applications
Lateral flow immunoassay.
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Background
CRP is an important protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by IL-1 and TNF Alpha and Beta. CRP levels increase dramatically and serve as a useful marker of inflammation in such conditions as bacterial infection, viral infections, rheumatoid arthritis, transplantation rejection, myocardial infarction, meningitis, septicemia, osteomyelitis and others. CRP is also correlated to Serum Amyloid A levels.
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Type
Mouse antibody Monoclonal.
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Purification Method
Purified monoclonal IgG1 by protein A 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.
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Name :
MMP12 Human (1-33)Description:
Matrix Metalloproteinase 12 (1-33 a.a.) Human Recombinant
Product # :
ENZ-1201Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The MMP12 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The MMP12 His-Tagged Fusion Protein, produced in E. coli, is a 10kDa protein containing 33 amino acid residues of the MMP12 Human, 1-33 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
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized MMP12 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.
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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.
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Amino Acid Sequence
MKFLLILLLQ ATASGALPLN SSTSLEKNNV LFG.
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Background
Matrix Metalloproteinase 12 also known as MMP12 is 1 of the main enzymes in the MMP family which is primarily produced by macrophages and neutrophils. MMP12 is implicated in the breakdown of elastin and in the development of chronic inflammatory diseases, such as emphysema, COPD and atherosclerosis. MMP12 is upregulated and contributes to tissue remodeling in inflammatory responses which is essential for wound healing and immune defense. MMP12 catalyzes the cleavage of collagen, elastin and other ECM components. Its activity is regulated in normal tissues to avoid pathological degradation.
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.
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Name :
Aprotinin ProteinDescription:
Aprotinin
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
Product # :
PRO-285Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Aprotinin is a natural proteinase inhibitor polypeptide consisting of fifty-eight amino acids {C284H432N84O79S7} arranged in a single polypeptide chain, cross-linked by three disulfide bridges and having a molecular mass of 6512.
Source
Bovine Lung.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
More Info
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Introduction
Aprotinin inhibits the activity of several proteolytic enzymes such as chymotrypsin, kallikrein, plasmin and trypsin. Aprotinin is present in blood and in most tissues, with a high concentration in lung. Aprotinin inhibits pro-inflammatory cytokine release and maintains glycoprotein homeostasis. In platelets, aprotinin reduces glycoprotein loss (e.g., GpIb, GpIIb/IIIa), while in granulocytes it prevents the expression of pro-inflammatory adhesive glycoproteins (e.g., CD11b).
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Synonyms
Pancreatic trypsin inhibitor, Basic protease inhibitor, BPI, BPTI, Aprotinin, AP.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Aprotinin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Aprotinin 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.
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Solubility
It is recommended to reconstitute the lyophilized Aprotinin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Specific Activity
5,940 KIU (Kallikrein Inactivator Units) per mg, 3.3 pH.Eur.U/mg.
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.
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Name :
T.gondii ROP4Description:
Toxoplasma Gondii ROP4 (RH2) Mosaic Recombinant
Product # :
TOX-266Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.coli derived recombinant artificial mosaic protein contains the ROP4 (RH2) immunodominant regions, the protein is fused to Glutathione transferase.
Source
Escherichia Coli.
Formulation
25mM Tris-HCl pH 8.0, 5mM Glutathione, 1.5M urea and 50% glycerol.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
The life cycle of Toxoplasma gondii has two phases. The coccidia like takes place only in members of the Felidae family which makes these animals the parasite's primary host. The asexual part of the life cycle can take place in any warm-blooded animal, like other mammals(including felines) and birds. T. gondii constructing daughter scaffolds within the mother cell. In the intermediate hosts (including felines), the parasite invades cells, forming intracellular so-called parasitophorous vacuoles containing bradyzoites, the slowly replicating form of the parasit. Vacuoles form tissue cysts mainly within the muscles and brain. Since they are within cells, the host's immune system does not detect these cysts. Resistance to antibiotics varies, but the cysts are very difficult to eradicate entirely. Within these vacuoles T. gondii propagates by a series of binary fissions until the infected cell eventually bursts and tachyzoites are released. Tachyzoites are the motile, asexually reproducing form of the parasite. Unlike the bradyzoites, the free tachyzoites are usually efficiently cleared by the host's immune response, although some manage to infect cells and form bradyzoites, thus maintaining the infection.
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Stability
Toxoplasma protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Toxoplasma antigen is suitable for ELISA and Western blots, excellent antigen for detection of Toxoplasma gondii- with minimal specificity problems.
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Specificity
Immunoreactive with sera of Toxoplasma gondii-infected individuals.
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Purification Method
Toxoplasma protein was purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TNNI3 Human ChimericDescription:
Cardiac Troponin-I Chimeric Human Recombinant
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Product # :
PRO-2790Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNNI3 Human Chimeric produced in E.Coli is a single, non-glycosylated polypeptide chain (28-110 a.a.) and having a molecular mass of 29072 Dalton.
Source
Escherichia Coli.
Formulation
TNNI3 was lyophilized in 50mM Tris-HCl, 5mM Calcium chloride, 0.7M KCl and 0.1% 2-mercaptoethanol, pH 7.5
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiac Troponin-I Chimeric although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 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.
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Solubility
It is recommended to reconstitute the lyophilized TNNI3 in buffer containing BSA not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Troponin I (TNNI3) is a crucial regulatory protein in cardiac muscle, playing a central role in the regulation of muscle contraction. Understanding the structure and function of TNNI3 is essential for unraveling the complexities of cardiac muscle physiology and exploring therapeutic interventions for cardiac diseases. Chimeric TNNI3 proteins, which combine segments from different isoforms or species, offer a unique opportunity to investigate the role of specific regions in TNNI3 function and to potentially develop novel therapies. This research aims to provide a comprehensive exploration of chimeric TNNI3 proteins, elucidating their functions, structural significance, and potential applications in cardiology and biomedical research.
The primary objective of this research is to elucidate the functional significance of chimeric TNNI3 proteins in cardiac muscle. In vitro and ex vivo experiments, utilizing engineered chimeric TNNI3 constructs and cardiac tissue models, will be conducted to investigate how these proteins influence muscle contractility, calcium sensitivity, and response to pathological conditions. Understanding these mechanisms is fundamental for deciphering the roles of specific TNNI3 regions in cardiac muscle function.
The second objective is to assess the therapeutic potential of chimeric TNNI3 proteins in cardiac diseases. Experimental studies involving animal models and cellular systems will explore the use of chimeric TNNI3 proteins as potential therapeutic agents for heart conditions. These investigations may provide valuable insights into novel treatment strategies targeting cardiac muscle function.
The third objective is to explore the broader applications of chimeric TNNI3 proteins in biotechnology and drug development. Research will investigate the use of chimeric TNNI3-expressing cells and tissues as models for studying cardiac disorders and for developing innovative approaches in regenerative medicine and pharmacology.
By delving into the functions and roles of chimeric TNNI3 proteins, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology, biotechnology, and drug development
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.
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Name :
TNNI3 Human NativeDescription:
Cardiac Troponin-I Human
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
Product # :
PRO-2788Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNNI3 Native produced in Human heart tissue is a full length protein which has an additional amino acid residues on its N terminus that are not present on the skeletal form, making this protein a promising analyte for indicating cardiac specificity.TNNI3 Native is purified by proprietary chromatographic technique.
Source
Human heart tissue.
Formulation
TNNI3 was lyophilized from 0.01M HCl.
Purity
Greater than 98.0% as determined by SDS-PAGE.
More Info
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Synonyms
Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Cardiac Troponin-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 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.
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Solubility
It is recommended to reconstitute the lyophilized TNNI3 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Troponin I, encoded by the TNNI3 gene, is a critical component of the troponin complex in cardiac muscle cells. It plays a central role in the regulation of cardiac muscle contraction by modulating the interaction between actin and myosin filaments.
While extensive research has been conducted on troponin I in the context of cardiac diseases, there is a growing need to investigate native human troponin I (TNNI3) in its unmodified form to gain a deeper understanding of its functions, structural significance, and implications for heart health. This research aims to provide a comprehensive exploration of TNNI3 in its native state, shedding light on its various roles and potential applications in cardiology and biomedical research.
The primary objective of this research is to elucidate the physiological role of native human TNNI3 in cardiac muscle contraction. Experiments involving human cardiac tissue samples and isolated myocytes will be conducted to investigate how TNNI3 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of cardiac muscle physiology and its implications for heart health.
The second objective is to assess the clinical relevance of native TNNI3 in cardiac diseases. Clinical studies involving patients with various cardiac conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI3 as a biomarker. These investigations may provide valuable insights into the use of native TNNI3 in the early detection and management of heart diseases.
The third objective is to explore the potential applications of native TNNI3 in biomedical research and drug development. Research will investigate the use of native TNNI3-expressing cells as models for studying cardiac disorders and for developing novel therapeutic interventions targeting the troponin complex.
By delving into the functions and roles of native human TNNI3, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology and biomedical 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.
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Name :
HPRT AntibodyDescription:
Hypoxanthine-Guanine Phosphoribosyltransferase, Mouse Anti Human
Hypoxanthine-Guanine Phosphoribosyltransferase, EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.
Product # :
ANT-046Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.
More Info
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Introduction
HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.
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Synonyms
Hypoxanthine-Guanine Phosphoribosyltransferase, EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.
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Immunogen
Anti-human HPRT mAb, is derived from hybridization of mouse FO myeloma cells with spleen cells from BALB/c mice immunized with recombinant human HPRT amino acids 1-218 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT2G8AT.
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Applications
HPRT antibody has been tested by ELISA and 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.
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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.
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Purification Method
HPRT 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.
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Name :
T.gondii p24Description:
Toxoplasma Gondii p24 (GRA1) Recombinant
Product # :
TOX-262Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.Coli derived recombinant protein contains the p24 (GRA1) immunodominant regions, fused to six histidines at C-terminal.
Source
Escherichia Coli.
Formulation
(1mg/ml) 1XPBS, pH 7.2 and 50% glycerol.
Purity
Toxoplasma protein is >90% pure as determined by SDS-PAGE.
More Info
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Introduction
The life cycle of Toxoplasma gondii has two phases. The coccidia like takes place only in members of the Felidae family which makes these animals the parasite's primary host. The asexual part of the life cycle can take place in any warm-blooded animal, like other mammals(including felines) and birds. T. gondii constructing daughter scaffolds within the mother cell. In the intermediate hosts (including felines), the parasite invades cells, forming intracellular so-called parasitophorous vacuoles containing bradyzoites, the slowly replicating form of the parasit. Vacuoles form tissue cysts mainly within the muscles and brain. Since they are within cells, the host's immune system does not detect these cysts. Resistance to antibiotics varies, but the cysts are very difficult to eradicate entirely. Within these vacuoles T. gondii propagates by a series of binary fissions until the infected cell eventually bursts and tachyzoites are released. Tachyzoites are the motile, asexually reproducing form of the parasite. Unlike the bradyzoites, the free tachyzoites are usually efficiently cleared by the host's immune response, although some manage to infect cells and form bradyzoites, thus maintaining the infection.
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Stability
Toxoplasma Protein although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SPARC HumanDescription:
Secreted Protein Acidic & Rich in Cysteine Recombinant Human
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
Product # :
PRO-2602Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Secreted Protein Acidic & Rich in Cysteine Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 286 amino acids and having a molecular mass of 32.7kDa.SPARC 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 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by its ability to inhibit the cell growth of Mv1Lu mink lung epithelial cells is < 3.0 µg/mL, corresponding to a specific activity of > 333 IU/mg.
More Info
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Introduction
SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.
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Synonyms
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPARC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Secreted Protein Acidic & Rich in Cysteine should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SPARC in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APQQEALPDE TEVVEETVAE VTEVSVGANP VQVEVGEFDD GAEETEEEVV AENPCQNHHC KHGKVCELDE NNTPMCVCQD PTSCPAPIGE FEKVCSNDNK TFDSSCHFFA TKCTLEGTKK GHKLHLDYIG PCKYIPPCLD SELTEFPLRM RDWLKNVLVT LYERDEDNNL LTEKQKLRVK KIHENEKRLE AGDHPVELLA RDFEKNYNMY IFPVHWQFGQ LDQHPIDGYL SHTELAPLRA PLIPMEHCTT RFFETCDLDN DKYIALDEWA GCFGIKQKDI DKDLVI.
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.
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Name :
CEL MouseDescription:
Carboxyl Ester Lipase Mouse Recombinant
Bile salt-activated lipase, BAL, EC 3.1.1.13, EC 3.1.1.3, Bile salt-stimulated lipase, BSSL, Bucelipase, Carboxyl ester lipase, Cholesterol esterase, Pancreatic lysophospholipase, Sterol esterase, CEL, FAP, BSDL, CELL, FAPP, LIPA, Cease, MODY8.
Product # :
ENZ-1115Price :
Quantity :
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Shipped with Ice Packs
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Description
CEL Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 585 amino acids (21-599 aa) and having a molecular mass of 64.5kDa.CEL is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The CEL solution (0.5 mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 100,000 pmol/min/ug. Measured by the amount of enzyme that hydrolyze 1.0 umole of p-nitrophenyl butyrate to p-nitrophenol per minute at pH7.5 at 25C˚.
More Info
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Introduction
Carboxyl ester lipase also known as CEL, formely called cholesterol esterase or bile salt-stimulated lipase, is an enzyme with lipolytic capablity of hydrolyzing cholesteryl esters, tri-, di-, and mono- phospholipids, acylglycerol, ceramide and lysophospholipids. The carboxyl terminus of the enzyme controls enzymatic activity by creating hydrogen bonds with the surface loop to partlyshield the active site. The active catalytic site triad of serine-histidine-aspartate is centrally located in the enzyme structure and is partly covered by a surface loop. Bile salt binding to the loop domain set free the active site for accessibility by water-insoluble substrates. CEL is produced mainly in the pancreas and lactating mammary gland, thus the protein is also expressed in liver, macrophages, and in the vessel wall.
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Synonyms
Bile salt-activated lipase, BAL, EC 3.1.1.13, EC 3.1.1.3, Bile salt-stimulated lipase, BSSL, Bucelipase, Carboxyl ester lipase, Cholesterol esterase, Pancreatic lysophospholipase, Sterol esterase, CEL, FAP, BSDL, CELL, FAPP, LIPA, Cease, MODY8.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
AKLGAVYTEG GFVEGVNKKL SLLGGDSVDI FKGIPFATAK TLENPQRHPG WQGTLKATNF
KKRCLQATIT QDNTYGQEDC LYLNIWVPQG RKQVSHNLPV MVWIYGGAFL MGSGQGANFL
KNYLYDGEEI ATRGNVIVVT FNYRVGPLGF LSTGDANLPG NFGLRDQHMA IAWVKRNIAA
FGGDPDNITI FGESAGAASV SLQTLSPYNK GLIRRAISQS GMALSPWAIQ KNPLFWAKTI
AKKVGCPTED TGKMAACLKI TDPRALTLAY KLPVKKQEYP VVHYLAFIPV IDGDFIPDDP
INLYNNTADI DYIAGINNMD GHLFATIDVP AVDKTKQTVT EEDFYRLVSG HTVAKGLKGA
QATFDIYTES WAQDPSQENM KKTVVAFETD VLFLIPTEIA LAQHKAHAKS AKTYSYLFSH
PSRMPIYPKW MGADHADDLQ YVFGKPFATP LGYRPQDRAV SKAMIAYWTN FARSGDPNMG
NSPVPTHWYP YTLENGNYLD ITKTITSASM KEHLREKFLK FWAVTFEVLP TVTGDQDTLT
PPEDDSEVAP DPPSDDSQVV PVPPTDDSVE AQMPATIGFH HHHHH
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.
- View Data Sheet
Name :
TNNT1 HumanDescription:
Slow Skeletal Troponin T Human Recombinant
Troponin T, slow skeletal muscle, TnTs, Slow skeletal muscle troponin T (sTnT), TNNT1, TNT.
Product # :
PRO-2791Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TNNT1 Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 278 a.a and having a molecular mass of 32948 Dalton.
Source
Escherichia Coli.
Formulation
TNNT1 was lyophilized in 0.01M HCl, pH 2.0.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Troponin T, slow skeletal muscle, TnTs, Slow skeletal muscle troponin T (sTnT), TNNT1, TNT.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Slow Skeletal Troponin T although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNT1 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.
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Solubility
It is recommended to reconstitute the lyophilized TNNT1 in buffer containing 0.01M HCl, pH 2.0 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
The Troponin T1 Slow Skeletal Type (TNNT1) human recombinant protein has emerged as a focal point in biomedical research, offering a key to unraveling the complexities of muscle contraction and its implications in neuromuscular disorders. TNNT1 is a critical component of the troponin complex, which regulates striated muscle contraction by controlling the interaction between actin and myosin. The TNNT1 human recombinant, synthesized through advanced biotechnological techniques, provides a valuable tool to explore the intricate molecular characteristics and functional roles of this essential protein.
Understanding the molecular characteristics of TNNT1 is fundamental to comprehending its role in muscle physiology and pathology. TNNT1, a slow skeletal muscle isoform, possesses unique structural features that enable its binding to tropomyosin, a key regulator of muscle contraction. The interactions between TNNT1, tropomyosin, and other troponin subunits are central to the fine-tuned regulation of muscle contraction.
TNNT1 is primarily expressed in slow-twitch skeletal muscles, which are responsible for sustained, endurance-type activities. The functional significance of TNNT1 lies in its role in modulating muscle contraction kinetics, allowing for prolonged muscle activity without fatigue. Moreover, TNNT1 mutations have been associated with congenital myopathies and neuromuscular disorders, emphasizing its crucial role in muscle health.
The TNNT1 human recombinant has promising implications for both research and potential therapeutic applications. Researchers can utilize this recombinant protein to investigate the structural and functional properties of TNNT1, shedding light on its interactions with other muscle proteins and its role in muscle diseases. Additionally, TNNT1-based therapies may hold the key to addressing neuromuscular disorders, providing hope for improved treatments and patient outcomes.
This research aims to provide a comprehensive analysis of the TNNT1 human recombinant, focusing on its molecular characteristics, functional significance, and potential therapeutic implications. By delving into the intricate nature of TNNT1, we aim to contribute to a deeper understanding of muscle biology and pave the way for future research and therapeutic advancements in the realm of neuromuscular disorders.
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.
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Name :
METAP1D HumanDescription:
Methionyl Aminopeptidase 1D Human Recombinant
MAP1D, Metap1l, Methionine aminopeptidase 1D, mitochondrial, MAP 1D, MetAP 1D, Methionyl aminopeptidase type 1D, mitochondrial, Peptidase M 1D, METAP1D.
Product # :
ENZ-759Price :
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Shipping Method :
Shipped with Ice Packs
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Description
METAP1D Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (20-335a.a) and having a molecular mass of 37.4kDa. METAP1D is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The METAP1D solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Methionyl Aminopeptidase 1D (METAP1D) is a part of the peptidase M24A family. METAP1D which is overexpressed in colon cancer cell lines participates in tumorigenesis. METAP1D eliminates methionine from the N-terminus of nascent proteins.
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Synonyms
MAP1D, Metap1l, Methionine aminopeptidase 1D, mitochondrial, MAP 1D, MetAP 1D, Methionyl aminopeptidase type 1D, mitochondrial, Peptidase M 1D, METAP1D.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSSPLNHI YLHKQSSSQQ RRNFFFRRQR DISHSIVLPA AVSSAHPVPK HIKKPDYVTT GIVPDWGDSI EVKNEDQIQG LHQACQLARH VLLLAGKSLK VDMTTEEIDA LVHREIISHN AYPSPLGYGG FPKSVCTSVN NVLCHGIPDS RPLQDGDIIN IDVTVYYNGY HGDTSETFLV GNVDECGKKL VEVARRCRDE AIAACRAGAP FSVIGNTISH ITHQNGFQVC PHFVGHGIGS YFHGHPEIWH HANDSDLPME EGMAFTIEPI ITEGSPEFKV LEDAWTVVSL DNQRSAQFEH TVLITSRGAQ ILTKLPHEA.
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.
- View Data Sheet
Name :
Adiponectin Human, HMWDescription:
Adiponectin glycosylated Human Recombinant, HMW Rich
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-764Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Adiponectin Human Recombinant HMW Rich produced in HEK cells is a single, glycosylated, polypeptide chain (19-244) containing a total of 226 amino acids, having a molecular mass of 24.6kDa (calculated). Human Acrp30 HMW Rich migrates on SDS-PAGE under non-reducing conditions at ~ 884 kDa.
Source
HEK293.
Formulation
Acrp30 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl, pH 7.5 and 1mM CaCl2.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.
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Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Acrp30 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
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Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 24.6 kDa.
What is the source or expression system of ADIPONECTIN Protein?
HEK293.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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.
- View Data Sheet
Name :
SPECC1 HumanDescription:
Sperm Antigen With Calponin Homology And Coiled-Coil 1 Human Recombinant
CYTSB, HCMOGT-1, HCMOGT1, NSP, Cytospin-B, Nuclear structure protein 5, NSP5, Sperm antigen HCMOGT-1, Sperm antigen with calponin homology and coiled-coil domains 1, SPECC1.
Product # :
PRO-2002Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SPECC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (458-761a.a) and having a molecular mass of 37.7kDa. SPECC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SPECC1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol 1mM DTT and 0.1M NaCl.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Sperm Antigen With Calponin Homology And Coiled-Coil 1 (SPECC1) which is a part of the cytospin-A family takes part in cytokinesis and spindle organization. SPECC1 takes part in actin cytoskeleton organization and microtubule stabilization and therefore necessary for proper cell adhesion and migration.
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Synonyms
CYTSB, HCMOGT-1, HCMOGT1, NSP, Cytospin-B, Nuclear structure protein 5, NSP5, Sperm antigen HCMOGT-1, Sperm antigen with calponin homology and coiled-coil domains 1, SPECC1.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTQEGKII ELEQKCTGIL EQGRFEREKL LNIQQQLTCS LRKVEEENQG ALEMIKRLKE ENEKLNEFLE LERHNNNMMA KTLEECRVTL EGLKMENGSL KSHLQGEKQK ATEASAVEQT AESCEVQEML KVARAEKDLL ELSCNELRQE LLKANGEIKH VSSLLAKVEK DYSYLKEICD HQAEQLSRTS LKLQEKASES DAEIKDMKET IFELEDQVEQ HRAVKLHNNQ LISELESSVI KLEEQKSDLE RQLKTLTKQM KEETEEWRRF QADLQTAVVV ANDIKCEAQQ ELRTVKRKLL EEEEKNA.
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.
- View Data Sheet
Name :
Borrelia DbpADescription:
Borrelia Burgdorferi Decorin Binding Protein A Recombinant
Product # :
BOR-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Borrelia Burgdorferi Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 19,916 Dalton. Borrelia DbpA is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Borrelia DbpA (0.91mg/1ml) is supplied in 20mM HEPES buffer pH-8.0 and 20% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Applications
Western blot with Lyme positive plasma.
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Patent Protected Countries
The Sale and/or commercial use of recombinant Borrelia DbpA by ProSpec is prohibited in the following countries: Canada, USA, Germany, Austria, Belgium, Switzerland, Denmark, Finland, France, United Kingdom, Ireland, Netherlands and Sweden.
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.
- View Data Sheet
Name :
CHST10 HumanDescription:
Carbohydrate Sulfotransferase 10 Human Recombinant
Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.
Product # :
ENZ-894Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CHST10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (28-356 a.a) and having a molecular mass of 41.2kDa.CHST10 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHST10 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Carbohydrate Sulfotransferase 10, also known as CHST10 is a member of the sulfotransferase 2 family. CHST10 was first recognized as a sulfotransferase which acts on the human natural killer-1 (HNK-1) glycan. Furthermore, CHST10 is a carbohydrate involved in neurodevelopment as well as synaptic plasticity.
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Synonyms
Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTFKDPDVYS AKQEFLFLTT MPEVRKLPEE KHIPEELKPT GKELPDSQLV QPLVYMERLE LIRNVCRDDA LKNLSHTPVS KFVLDRIFVC DKHKILFCQT PKVGNTQWKK VLIVLNGAFS SIEEIPENVV HDHEKNGLPR LSSFSDAEIQ KRLKTYFKFF IVRDPFERLI SAFKDKFVHN PRFEPWYRHE IAPGIIRKYR RNRTETRGIQ FEDFVRYLGD PNHRWLDLQF GDHIIHWVTY VELCAPCEIM YSVIGHHETL EDDAPYILKE AGIDHLVSYP TIPPGITVYN RTKVEHYFLG ISKRDIRRLY ARFEGDFKLF GYQKPDFLLN.
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.
- View Data Sheet
Name :
M.Pneumoniae P1-CDescription:
Mycoplasma Pneumoniae P1-C Recombinant
Product # :
PRO-801Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The Recombinant Mycoplasma Pneumoniae C-terminal region (P1C) of the P1 protein was expressed in E. coli containing 362 amino acids. The protein is fused to a 6 His Tag. This peptide can be used as an antigen in the diagnosis of M. pneumoniae infection.
Source
E.Coli
Formulation
Mycoplasma Pneumoniae P1-C is formulated in 1x PBS pH 7.4.
Purity
Greater than 95% as determined by 12% PAGE (Coomassie staining).
More Info
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Introduction
Mycoplasma pneumonia is part of the atypical pneumonia subtype which is caused by the bacteria M. pneumoniae. Mycoplasma pneumonia affects individuals younger than 40. It makes up 15 - 50% of all pneumonia cases in adults and especially in school-aged children. People at great risk for mycoplasma pneumonia comprise of those living or working in busy areas such as schools and homeless shelters, although many people who contract mycoplasma pneumonia have no identifiable risk factor. P1, P30, and P116 of mycoplasma pneumonia membrane proteins have been recognized as adhensive factors, P1 is considered as a main adhension protein of the organism colonization.
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Physical Appearance
Streile filtered colorless solution.
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Stability
Upon arrival, Store at -20°C.Please prevent freeze-thaw cycles.
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Applications
Immunoassay.
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Purification Method
The recombinant fusion protein was purified by GSH affinity chromatography technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Malaria Pf. MSP1Description:
Malaria Falciparum MSP1 Recombinant
Product # :
MAL-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Merozoite surface antigen is a protein located on the outside of the merozoite, playing an imperative role in immune reaction. About 55% cases of malaria are infected by Plasmodium falciparum (Pf). Pf MSP1 has to be used with Plasmodium vivax (Pv) together for ELISA and rapid diagnostic test, Plasmodium falciparum and vivax infection takes about 95% of Plasmodium caused infection. Recombinant Malaria Falciparum MSP1 produced in E.coli, is a 62kDa protein fused to a GST tag at N-terminus and purified by proprietary chromatographic technique.
Formulation
Sterile Filtered solution containing PBS and 25mM K2CO3.
Purity
Protein is >90% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
Plasmodium falciparum is a protozoan parasite, one of the species of Plasmodium that cause malaria. Malaria parasites are members of the Apicomplexa. Apicomplexa are characterized by a set of organelles found in some stages of the parasite's life cycle. These organelles, collectively known as apical organelles because of their localization at one end of the parasite, are involved in interactions between the parasite and host. In particular, the apical organelles have been implicated in the process of host cell invasion. In the case of Plasmodium, three distinct invasive forms have been identified: sporozoite, merozoite, and ookinete.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Pf. MSP1 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Applications
Rapid test and Immunoassay.
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.
- View Data Sheet
Name :
MIP 1a HumanDescription:
Macrophage Inflammatory Protein-1 Alpha Human Recombinant (CCL3)
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.
Product # :
CHM-233Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Macrophage Inflammatory Protein-1 alpha Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from 0.55 mg/ml solution containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
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Introduction
Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophilsand basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.
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Synonyms
Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 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.
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Solubility
It is recommended to reconstitute the lyophilized Macrophage Inflammatory Protein-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Ser-Leu-Ala-Ala.
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Background
What is the molecular weight/Mw of MIP 1A HUMAN Protein?
MIP 1A HUMAN Protein has a total Mw of 7.82kDa.
What is the source or expression system of MIP 1A HUMAN Protein?
Escherichia Coli.
What is the Purity of MIP 1A HUMAN Protein?
MIP 1A HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of MIP 1A HUMAN Protein?
The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of MIP 1A HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Ser-Leu-Ala-Ala.
What applications can MIP 1A HUMAN Protein be used in?
MIP 1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for MIP 1A HUMAN Protein?
The endotoxin level is minimal, MIP 1A HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ADH6 HumanDescription:
Alcohol Dehydrogenase 6 Human Recombinant
Alcohol dehydrogenase 6, ADH6, ADH-5.
Product # :
ENZ-619Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ADH6 Human Recombinant produced E. coli is a single polypeptide chain containing 399 amino acids (1-375) and having a molecular mass of 42.4kDa.ADH6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The ADH6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Alcohol dehydrogenase 6 (ADH6) belongs to the alcohol dehydrogenase family. Alcohol dehydrogenase family members metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH6 is expressed in the stomach as well as in the liver, and it contains a glucocorticoid response element upstream of its 5’ UTR, which is a steroid hormone receptor binding site.
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Synonyms
Alcohol dehydrogenase 6, ADH6, ADH-5.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSTTGQ VIRCKAAILW KPGAPFSIEE VEVAPPKAKE VRIKVVATGL CGTEMKVLGS KHLDLLYPTI LGHEGAGIVE SIGEGVSTVK PGDKVITLFL PQCGECTSCL NSEGNFCIQF KQSKTQLMSD GTSRFTCKGK SIYHFGNTST FCEYTVIKEI SVAKIDAVAP LEKVCLISCG FSTGFGAAIN TAKVTPGSTC AVFGLGGVGL SVVMGCKAAG AARIIGVDVN KEKFKKAQEL GATECLNPQD LKKPIQEVLF DMTDAGIDFC FEAIGNLDVL AAALASCNES YGVCVVVGVL PASVQLKISG QLFFSGRSLK GSVFGGWKSR QHIPKLVADY MAEKLNLDPL ITHTLNLDKI NEAVELMKTG KCIRCILLL.
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.
- View Data Sheet
Name :
HLA-DOA HumanDescription:
Major Histocompatibility Complex Class II DO Alpha Human Recombinant
HLA-DNA, HLA-DZA, HLADZ, HLA class II histocompatibility antigen, DO alpha chain, MHC DN-alpha, MHC DZ alpha, MHC class II antigen DOA, HLA-DOA.
Product # :
PRO-1535Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HLA-DOA Human Recombinant produced in E. coli is a single polypeptide chain containing 215 amino acids (26-217) and having a molecular mass of 24.1kDa. HLA-DOA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HLA-DOA solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Major Histocompatibility Complex Class II DO Alpha (HLA-DOA) is a significant modulator in the HLA class II restricted antigen presentation pathway by interaction with the HLA-DM molecule in B-cells. HLA-DOA forms a heterodimer along with HLA-DOB. The heterodimer is located in lysosomes in B cells and regulates HLA-DM-mediated peptide loading on MHC class II molecules. HLA-DOA exhibits very little sequence variation, particularly at the protein level.
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Synonyms
HLA-DNA, HLA-DZA, HLADZ, HLA class II histocompatibility antigen, DO alpha chain, MHC DN-alpha, MHC DZ alpha, MHC class II antigen DOA, HLA-DOA.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTKADHMG SYGPAFYQSY GASGQFTHEF DEEQLFSVDL KKSEAVWRLP EFGDFARFDP QGGLAGIAAI KAHLDILVER SNRSRAINVP PRVTVLPKSR VELGQPNILI CIVDNIFPPV INITWLRNGQ TVTEGVAQTS FYSQPDHLFR KFHYLPFVPS AEDVYDCQVE HWGLDAPLLR HWELQVPIPP PDAME.
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.