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1000 results found for “Karyopherin”
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Name :
Thrombopoietin HumanDescription:
Thrombopoietin Human Recombinant
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO
Product # :
CYT-1178Price :
Quantity :
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Shipped with Ice Packs
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Description
TPO Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain containing 343 amino acids (22-353 a.a) and having a molecular mass of 36.8kDa.TPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
TPO protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range is ≤10ng/ml. It is measured by cell proliferation assay using MO7e human megakaryocytic leukemic cells.
More Info
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Introduction
Thrombopoietin is a glycoprotein hormone produced mainly by the liver and the kidney which regulates the production of platelets by the bone marrow. TPO stimulates the production as well as differentiation of megakaryocytes, the bone marrow cells which fragment into large numbers of platelets.
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Synonyms
Megakaryocyte colony-stimulating factor, Myeloproliferative leukemia virus oncogene ligand, C-mpl ligand, ML, Megakaryocyte growth and development factor, MGDF, TPO, MKCSF, MPLLG, MGC163194, THPO
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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
DGSHMSPAPP ACDLRVLSKL LRDSHVLHSR LSQCPEVHPL PTPVLLPAVD FSLGEWKTQM EETKAQDILG AVTLLLEGVM AARGQLGPTC LSSLLGQLSG QVRLLLGALQ SLLGTQLPPQ GRTTAHKDPN AIFLSFQHLL RGKVRFLMLV GGSTLCVRRA PPTTAVPSRT SLVLTLNELP NRTSGLLETN FTASARTTGS GLLKWQQGFR AKIPGLLNQT SRSLDQIPGY LNRIHELLNG TRGLFPGPSR RTLGAPDISS GTSDTGSLPP NLQPGYSPSP THPPTGQYTL FPLPPTLPTP VVQLHPLLPD PSAPTPTPTS PLLNTSYTHS QNLSQEGHHH HHH
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 :
Cyclophilin A RatDescription:
Cyclophilin-A Rat Recombinant
Peptidyl-prolyl cis-trans isomerase A, EC:5.2.1.8, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, p1B15, p31, Ppia.
Product # :
ENZ-938Price :
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Shipped at Room temp
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Description
Cyclophilin-A Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Val2-Leu164) containing 173 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 19kDa.
Source
Escherichia Coli.
Formulation
Cyclophilin-A was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline and 5%(w/v) trehalose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidyl-prolyl cis-trans isomerase A, EC:5.2.1.8, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, p1B15, p31, Ppia.
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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; 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. Cyclophilin-A 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
MKHHHHHHASVNPTVFFDIT ADGEPLGRVC FELFADKVPK TAENFRALST GEKGFGYKGS SFHRIIPGFM CQGGDFTRHN GTGGKSIYGE KFEDENFILK HTGPGILSMA NAGPNTNGSQ FFICTAKTEW LDGKHVVFGK VKEGMSIVEA MERFGSRNGK TSKKITISDC GQL.
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 :
KLK3, HisDescription:
Kallikrein-3 Human Recombinant, His Tag
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
Product # :
ENZ-620Price :
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Shipped with Ice Packs
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Description
KLK3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (25-261) and having a molecular mass of 28.8kDa.The KLK3 is fused to a 25 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
KLK3 protein solution (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH8.0) and 0.4M Urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Kallikrein-3 (KLK3) belongs to the kallikrein-related peptidase family. Kallikreins are a subgroup of serine proteases having various physiological functions. Numerous kallikreins are involved in carcinogenesis and some may be prospective cancer and other disease biomarkers. Kallikrein-3 is 1 of the 15 kallikrein subfamily members located in a cluster on chromosome 19 and is a protease present in seminal plasma. KLK3 hydrolyzes semenogelin-1 consequently leading to the liquefaction of the seminal coagulum. KLK3 is assumed to act normally in the liquefaction of seminal coagulum, probably by hydrolysis of the high molecular mass seminal vesicle protein. Serum level of the KLK3 protein, called PSA in the clinical setting, is beneficial in the diagnosis and monitoring of prostatic carcinoma.
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Synonyms
Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1.
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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 MGSHMIVGGW ECEKHSQPWQ VLVASRGRAV CGGVLVHPQW VLTAAHCIRN KSVILLGRHS LFHPEDTGQV FQVSHSFPHP LYDMSLLKNR FLRPGDDSSH DLMLLRLSEP AELTDAVKVM DLPTQEPALG TTCYASGWGS IEPEEFLTPK KLQCVDLHVI SNDVCAQVHP QKVTKFMLCA GRWTGGKSTC SGDSGGPLVC NGVLQGITSW GSEPCALPER PSLYTKVVHY RKWIKDTIVA NP.
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 :
PPIL3 HumanDescription:
Cyclophilin-J Human Recombinant
Peptidyl-prolyl cis-trans isomerase-like 3, PPIase, Cyclophilin J, CyPJ, Cyclophilin-like protein PPIL3, Rotamase PPIL3, PPIL3.
Product # :
ENZ-174Price :
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Shipped with Ice Packs
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Description
PPIL3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (1-161 a.a.) and having a molecular mass of 20.3kDa.PPIL3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PPIL3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 280 nmoles/min/mg, 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
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Introduction
Peptidyl-prolyl cis-trans isomerase-like 3 (PPIL3) belongs to the cyclophilin family which catalyzes the cis-trans isomerization of peptidylprolyl imide bonds in oligopeptides. PPIL3 acts either as catalyst or as molecular chaperone in protein-folding events.
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Synonyms
Peptidyl-prolyl cis-trans isomerase-like 3, PPIase, Cyclophilin J, CyPJ, Cyclophilin-like protein PPIL3, Rotamase PPIL3, PPIL3.
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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 MSVTLHTDVG DIKIEVFCER TPKTCENFLA LCASNYYNGC IFHRNIKGFM VQTGDPTGTG RGGNSIWGKK FEDEYSEYLK HNVRGVVSMA NNGPNTNGSQ FFITYGKQPH LDMKYTVFGK VIDGLETLDE LEKLPVNEKT YRPLNDVHIK DITIHANPFA Q.
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 :
PSPN HumanDescription:
Persephin Human Recombinant
Persephin, PSP, PSPN.
Product # :
CYT-801Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
PSPN Human Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.5kDa. The PSPN is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 10ng/ml, corresponding to a specific activity of > 1.0 × 100,000 IU/mg.More Info
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Introduction
Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.
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Synonyms
Persephin, PSP, PSPN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized PSPN although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PSPN 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 PSPN in 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
ALSGPCQLWS LTLSVAELGL GYASEEKVIF RYCAGSCPRG ARTQHGLALA RLQGQGRAHG GPCCRPTRYT DVAFLDDRHR WQRLPQLSAA ACGCGG.
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 :
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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 :
CMV Pp52Description:
Cytomegalo Virus Pp52 (UL44) Recombinant
Product # :
CMV-214Price :
Quantity :
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Shipped with Ice Packs
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Description
The E.coli derived 51 kDa recombinant protein contains the CMV Pp52 (UL44) immunodominant regions, 202-434 amino acids. Recombinant CMV-Pp52 is fused to a 26 kDa GST tag.
Source
Escherichia Coli.
Formulation
50mM Tris pH 7.2, 1mM EDTA and 50% glycerol.
Purity
CMV Pp52 protein is >95% pure as determined by 10% PAGE (coomassie staining).
More Info
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Introduction
CMV belongs to the Betaherpesvirinae subfamily of Herpesviridae which includes herpes simplex virustypes 1 and 2, varicella-zoster virus, and Epstein-Barrvirus. The herpesviruses share a characteristic ability to remain latentover long periods. CMV is a double-stranded linear DNA virus with 162 hexagonal protein capsomeres surrounded by a lipid membrane. CMV has the largest genome of the herpes viruses, ranging from 230-240 kilobase pairs. Human CMV is composed of unique and inverted repeats that include the existence of 4 genome isomers caused by inversion of L-S genome components (class E). Replication may be divided into immediate early, delayed early, and late gene expression based on time of synthesis after infection. The DNA is replicated by rolling circles. In vitro, CMV replicates in human fibroblasts.
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Stability
CMV Pp52 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
CMV Pp52 antigen is suitable for ELISA and Western blots, excellent antigen for detection of CMV with minimal specificity problems.
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Specificity
Immunoreactive with sera of CMV-infected individuals.
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Purification Method
CMV Pp52 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 :
HTF HumanDescription:
Holo Transferrin Human
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
Product # :
PRO-315Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Holo Transferrin is a glycoprotein of approximately 77 kDa.
Source
Human serum.
Formulation
The protein (10mg/ml) was lyophilized from 20mM NH4HC03 solution.
May contain traces of buffer salts.Purity
Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.
More Info
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Holo Transferrin, HTF.
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Physical Appearance
Sterile Filtered Pink lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Holo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin 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 Holo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, HBc, HBV, HAV, HIV and Syphilis.
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Iron Content
The Iron content was estimated by ICP and was found to be 1232 ppm.
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 :
FCAR HumanDescription:
Fc Fragment Of IgA Receptor Human Recombinant
Fc Fragment Of IgA Receptor, Fc Fragment Of IgA, Receptor For, CD89, Immunoglobulin Alpha Fc Receptor, Fc Alpha Receptor, FCAR Variant 14, IgA Fc Receptor, CD89 Antigen, CTB-61M7.2, FcalphaRI, Immunoglobulin alpha Fc receptor, IgA Fc receptor.
Product # :
PRO-2471Price :
Quantity :
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Shipped with Ice Packs
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Description
FCAR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 215 amino acids (22-227a.a.) and having a molecular mass of 24.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).FCAR is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
FCAR protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Fc Fragment Of IgA Receptor, also known as FCAR, is part of the multichain immune recognition receptor family which is the most abundant immunoglobulin in mucosal areas however it is only the second most common antibody isotype in serum. FCAR participates in both pro-and anti-inflammatory responses depending on the state of IgA bound. FCAR is also a vital Fc receptor for neutrophil killing of tumor cells. Once FCAR expressing neutrophils interact with IgA-opsonized tumor cells, the neutrophils not only show antibody-dependent cell-mediated cytotoxicity, but also release the cytokines TNF-α and IL-1β which cause increased neutrophil migration to the site.
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Synonyms
Fc Fragment Of IgA Receptor, Fc Fragment Of IgA, Receptor For, CD89, Immunoglobulin Alpha Fc Receptor, Fc Alpha Receptor, FCAR Variant 14, IgA Fc Receptor, CD89 Antigen, CTB-61M7.2, FcalphaRI, Immunoglobulin alpha Fc receptor, IgA Fc receptor.
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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
ADPQEGDFPM PFISAKSSPV IPLDGSVKIQ CQAIREAYLT QLMIIKNSTY REIGRRLKFW NETDPEFVID HMDANKAGRY QCQYRIGHYR FRYSDTLELV VTGLYGKPFL SADRGLVLMP GENISLTCSS AHIPFDRFSL AKEGELSLPQ HQSGEHPANF SLGPVDLNVS GIYRCYGWYN RSPYLWSFPS NALELVVTDS IHQDYTTQNH 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.
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Name :
C7ORF49 HumanDescription:
Chromosome 7 Open Reading Frame 49 Human Recombinant
MRI, Modulator of retrovirus infection homolog, C7orf49.
Product # :
PRO-1415Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
C7ORF49 Human Recombinant produced in E. coli is a single polypeptide chain containing 180 amino acids (1-157) and having a molecular mass of 19.2kDa. C7ORF49 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The C7ORF49 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Chromosome 7 Open Reading Frame 49 (C7ORF49) is affiliated with the lncRNA class. C7ORF49 characterizes the hamster ortholog and suggests that it may modulate the ability of the proteasome to degrade retroviral cores upon cellular infection.
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Synonyms
MRI, Modulator of retrovirus infection homolog, C7orf49.
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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 MGSMETLQSE TKTRVLPSWL TAQVATKNVA PMKAPKRMRM AAVPVAAARL PATRTVYCMN EAEIVDVALG ILIESRKQEK ACEQPALAGA DNPEHSPPCS VSPHTSSGSS SEEEDSGKQA LAPGLSPSQR PGGSSSACSR SPEEEEEEDV LKYVREIFFS.
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 :
KCTD5 HumanDescription:
Potassium Channel Tetramerisation Domain Containing 5 Human Recombinant
BTB/POZ domain-containing protein KCTD5, KCTD5.
Product # :
PRO-1276Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
KCTD5 Human Recombinant produced in E. coli is a single polypeptide chain containing 257 amino acids (1-234) and having a molecular mass of 28.5 kDa. KCTD5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The KCTD5 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
BTB/POZ domain-containing protein KCTD5 (KCTD5), is a 234 amino acid protein which localizes mainly in the cytoplasm however translocates to the nucleus on interaction with REP proteins. The expression of KCTD5 is up regulated post-transcriptionally in peripheral blood lymphocytes stimulated via the T-cell receptor. KCTD5 interacts particularly with cullin3, attaches ubiquitinated proteins, and created oligomers through its BTB domain.
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Synonyms
BTB/POZ domain-containing protein KCTD5, KCTD5.
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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 MGSMAENHCE LLSPARGGIG AGLGGGLCRR CSAGLGALAQ RPGSVSKWVR LNVGGTYFLT TRQTLCRDPK SFLYRLCQAD PDLDSDKDET GAYLIDRDPT YFGPVLNYLR HGKLVINKDL AEEGVLEEAE FYNITSLIKL VKDKIRERDS KTSQVPVKHV YRVLQCQEEE LTQMVSTMSD GWKFEQLVSI GSSYNYGNED QAEFLCVVSK ELHNTPYGTA SEPSEKAKIL QERGSRM
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 :
SERPINA3 HumanDescription:
Alpha-1 AntiChymotrypsin Human
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
Product # :
PRO-378Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Alpha-1 AntiChymotrypsin produced from normal human serum having a molecular mass of 68kDa.
Source
Human Serum.
Formulation
Lyophilized from 0.02M Tris-buffer,pH-7.5 and 0.15M Nacl.
Purity
Greater than 90.0%.
More Info
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Introduction
Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1- ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT. -
Synonyms
Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Human SERPINA3 although stable at room temperature for 3 weeks, should be stored between 2-8°C. Do not freeze.
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Solubility
It is recommended to reconstitute the lyophilized human A1ACT in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.
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 :
Cyclophilin-E AntibodyDescription:
Cyclophilin-E, Mouse Anti Human
Peptidyl-prolyl cis-trans isomerase E, PPIase E, Rotamase E, Cyclophilin-33, PPIE, peptidylprolyl isomerase E, CYP33, Cyclophilin E, CYP-33, MGC3736, MGC111222.
Product # :
ANT-695Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
Cyclophilin-E is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-E contains a highly conserved cyclophilin domain in addition to a RNA-binding domain. Cyclophilin-E exhibits PPIase activity, protein folding activities and possess RNA-binding activity. Cyclophilin-E contains 2 RNA binding domains at the N-terminal region and a PPIase domain at the C-terminal region.
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Synonyms
Peptidyl-prolyl cis-trans isomerase E, PPIase E, Rotamase E, Cyclophilin-33, PPIE, peptidylprolyl isomerase E, CYP33, Cyclophilin E, CYP-33, MGC3736, MGC111222.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human Cyclophilin-E mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Cyclophilin-E amino acids 1-301 purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
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Clone
PAT17E8AT.
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Applications
Cyclophilin-E 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.
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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
Cyclophilin-E 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.
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Name :
ARTN HumanDescription:
Artemin Human Recombinant
ART, ARTN , EVN, NBN.
Product # :
CYT-306Price :
Quantity :
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Shipped at Room temp
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Description
Artemin Human Recombinant produced in E.Coli is a disulfide-linked homodimer, non-glycosylated, polypeptide chain containing 2 x 113 amino acids and having a total molecular mass of 24.2 kDa. Artemin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Artemin was lyophilized after extensive dialysis against 10mM sodium citrate pH-4.5 and 25mM sodium chloride.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.More Info
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Introduction
The protein encoded by this gene is a member of the glial cell line-derived neurotophic factor (GDNF) family of ligands which are a group of ligands within the TGF-beta superfamily of signaling molecules. GDNFs are unique in having neurotrophic properties and have potential use for gene therapy in neurodegenrative disease. Artemin has been shown in culture to support the survival of a number of periferal neuron populations and at least one population of dopaminergic CNS neurons. Its role in the PNS and CNS is further substantiated by its expression pattern in the proximity of these neurons. This protein is a ligand for the RET receptor and uses GFR-alpha 3 as a coreceptor. Four alternatively spliced transcripts have been described, two of which encode the same protein.
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Synonyms
ART, ARTN , EVN, NBN.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Artemin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Artemin Human Recombinant 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 Artemin 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
AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.
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Background
Artemin Human Recombinant: Unraveling its Role in Neurobiology and Therapeutic Applications
Abstract:
Artemin, a member of the glial cell line-derived neurotrophic factor (GDNF) family, holds significant potential in neurobiology and therapeutic interventions. This research paper provides an overview of Artemin human recombinant, elucidating its molecular characteristics, signaling pathways, and therapeutic implications in neurological disorders. Understanding the multifaceted role of Artemin offers new avenues for targeted therapies. This article offers a concise analysis of Artemin, highlighting its impact on neurobiology and its therapeutic applications.
Introduction:
Neurological disorders represent a major challenge in healthcare, necessitating innovative therapeutic strategies. Artemin, a member of the GDNF family, has emerged as a promising molecule in neurobiology. This paper provides an overview of Artemin, shedding light on its structure, function, and therapeutic potential.
Artemin Signaling and Mechanisms:
Artemin binds to its receptor, Ret tyrosine kinase, and activates downstream signaling pathways, including the PI3K/AKT and MAPK pathways. These signaling cascades play crucial roles in neuronal survival, growth, and differentiation, highlighting the significance of Artemin in neurodevelopment and neuroprotection.
Artemin in Neurological Disorders:
Artemin has been implicated in various neurological disorders, including peripheral neuropathies and neurodegenerative diseases. Its neuroprotective properties and ability to enhance neuronal survival and regeneration make it a promising target for therapeutic interventions. Furthermore, Artemin may play a role in pain modulation and sensory neuron function.
Therapeutic Potential of Artemin Human Recombinant:
Artemin human recombinant offers promising prospects in the field of neurotherapeutics. Strategies aimed at modulating Artemin signaling or delivering exogenous Artemin hold potential for promoting neuronal survival, regeneration, and functional recovery. Artemin-based therapies could be developed for a range of neurological disorders, including peripheral neuropathies, Parkinson's disease, and spinal cord injuries.
Challenges and Future Directions:
While the therapeutic targeting of Artemin shows promise, several challenges lie ahead. Further research is needed to understand the precise mechanisms underlying Artemin's effects and its interactions with other signaling pathways. Additionally, the development of effective delivery methods and the identification of patient subgroups that may benefit from Artemin-based therapies are important considerations for clinical translation.
Conclusion:
Artemin human recombinant represents a promising avenue for therapeutic interventions in neurological disorders. Understanding the molecular mechanisms and functional implications of Artemin in neurobiology offers new opportunities for developing innovative treatments. Continued research in this field has the potential to improve the lives of individuals affected by neurological conditions and advance the field of neurotherapeutics.
What is the molecular weight/Mw of ARTN Protein?
ARTN Protein has a total Mw of 24.2kDa.
What is the source or expression system of ARTN Protein?
Escherichia Coli.
What is the Purity of ARTN Protein?
ARTN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of ARTN Protein?
The activity is determined by the dose-dependent proliferation of the SH-SY5Y cell line and is typically 4-8 ng/mL. The activity can also be determined by its ability to promote survival and neurite outgrowth.
What is the amino acid sequence of ARTN Protein?
AGGPGSRARA AGARGCRLRS QLVPVRALGL GHRSDELVRF RFCSGSCRRA RSPHDLSLAS LLGAGALRPP PGSRPVSQPC CRPTRYEAVS FMDVNSTWRT VDRLSATACG CLG.
What applications can ARTN Protein be used in?
ARTN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ARTN Protein?
The endotoxin level is minimal, ARTN 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.
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Name :
ASB8 HumanDescription:
Ankyrin Repeat And SOCS Box Containing 8 Human Recombinant
Ankyrin Repeat And SOCS Box Containing 8, ASB-8.
Product # :
PRO-1709Price :
Quantity :
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Shipped with Ice Packs
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Description
ASB8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 311 amino acids (1-288) and having a molecular mass of 34.0kDa.ASB8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ASB8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ASB8 is a substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin-protein ligase complex that facilitates the ubiquitination and consequent proteasomal degradation of objective proteins.
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Synonyms
Ankyrin Repeat And SOCS Box Containing 8, ASB-8.
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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 MGSMSSSMWY IMQSIQSKYS LSERLIRTIA AIRSFPHDNV EDLIRGGADV NCTHGTLKPL HCACMVSDAD CVELLLEKGA EVNALDGYNR TALHYAAEKD EACVEVLLEY GANPNALDGN RDTPLHWAAF KNNAECVRAL LESGASVNAL DYNNDTPLSW AAMKGNLESV SILLDYGAEV RVINLIGQTP ISRLVALLVR GLGTEKEDSC FELLHRAVGH FELRKNGTMP REVARDPQLC EKLTVLCSAP GTLKTLARYA VRRSLGLQYL PDAVKGLPLP ASLKEYLLLL 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.
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Name :
SYT4 HumanDescription:
Synaptotagmin IV Human Recombinant
HsT1192, KIAA1342, Synaptotagmin-4, Synaptotagmin IV, SytIV, SYT4.
Product # :
PRO-1375Price :
Quantity :
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Shipped with Ice Packs
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Description
SYT4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (38-425a.a) and having a molecular mass of 46.1kDa. SYT4 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SYT4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Synaptotagmin-4 (SYT4) is a part of the synaptotagmin proteins family. Synaptotagmins are a large gene family of synaptic vesicle type III integral membrane proteins that operate as regulators of both exocytosis and endocytosis and are involved in neurotransmitter secretion from small secretory vesicles. SYT4 is expressed in neuronal tissues, and has the highest mRNA levels in the hippocampus. The proximity of the SYT4 gene to markers of several psychiatric disorders implies an involvement of SYT4 in human disease such as pheochromocytoma, and parkinson's disease.
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Synonyms
HsT1192, KIAA1342, Synaptotagmin-4, Synaptotagmin IV, SytIV, SYT4.
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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 MCQRKSSKSN KTPPYKFVHV LKGVDIYPEN LNSKKKFGAD DKNEVKNKPA VPKNSLHLDL EKRDLNGNFP KTNLKPGSPS DLENATPKLF LEGEKESVSP ESLKSSTSLT SEEKQEKLGT LFFSLEYNFE RKAFVVNIKE ARGLPAMDEQ SMTSDPYIKM TILPEKKHKV KTRVLRKTLD PAFDETFTFY GIPYTQIQEL ALHFTILSFD RFSRDDIIGE VLIPLSGIEL SEGKMLMNRE IIKRNVRKSS GRGELLISLC YQSTTNTLTV VVLKARHLPK SDVSGLSDPY VKVNLYHAKK RISKKKTHVK KCTPNAVFNE LFVFDIPCEG LEDISVEFLV LDSERGSRNE VIGQLVLGAA AEGTGGEHWK EICDYPRRQI AKWHVLCDG.
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 :
Thyroglobulin HumanDescription:
Thyroglobulin Human Recombinant
Thyroglobulin, TGN, AITD3, TG.
Product # :
PRO-2803Price :
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Shipped at Room temp
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Description
Thyroglobulin Human produced in a mammalian cell line is a single, non-glycosylated polypeptide chain (1-2768 a.a.) and having a molecular mass of 304640 Dalton. Thyroglobulin Human is fused with GlyAlaProGly4SerHis10-tag at C-terminal and purified by proprietary chromatographic techniques.
Source
Mammalian cell line.
Formulation
Thyroglobulin was lyophilized from PBS, pH 7.4 and 5.4 % sucrose.
Purity
Greater than 95.0% as determined by SDS-PAGE.
sds-page
More Info
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Synonyms
Thyroglobulin, TGN, AITD3, TG.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thyroglobulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thyroglobulin 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 Thyroglobulin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Thyroglobulin, a glycoprotein primarily produced in the thyroid gland, stands at the center of thyroid hormone synthesis. Comprising a series of tyrosine residues, thyroglobulin serves as the scaffold upon which thyroid hormones are assembled. Beyond its pivotal role in thyroid physiology, thyroglobulin has garnered significant attention in the realm of thyroid disease diagnostics, offering valuable insights into thyroid function and disorders. This research delves into the intricacies of thyroglobulin human recombinant protein, exploring its biochemical properties, physiological significance, and its crucial applications in both clinical and research settings.
Structural Complexity of Thyroglobulin:
Thyroglobulin is a large, dimeric protein boasting an intricate structure composed of multiple domains. Within its structure lie tyrosine residues crucial for iodine incorporation, a process fundamental for thyroid hormone synthesis. Its size and complexity reflect the sophistication of thyroid hormone production, as thyroglobulin acts as a reservoir for thyroid hormones within the thyroid follicles.
Physiological Significance in Thyroid Function:
Thyroglobulin plays a central role in the synthesis of triiodothyronine (T3) and thyroxine (T4), the thyroid hormones essential for regulating metabolism and overall body homeostasis. During thyroid hormone synthesis, thyroglobulin is secreted into the follicular lumen, where it undergoes iodination and subsequent proteolysis, releasing T3 and T4. This process highlights the indispensable nature of thyroglobulin in thyroid hormone production, making it a key biomolecule in thyroid physiology.
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 :
AMH (452-560) HumanDescription:
Anti-Mullerian Hormone (452-560) Human Recombinant
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
Product # :
PRO-2843Price :
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Description
Anti-Mullerian Hormone Human Recombinant produced in CHO is a Homodimer, glycosylated, polypeptide chain containing 109 amino acids (Ser452-Arg560) and having a total molecular mass of 23.4Da.
Anti-Mullerian Hormone is purified by proprietary chromatographic techniques.
Source
CHO Cells.
Formulation
AMH Lyophilized from a 0.2µm filtered solution in 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.
Purity
Greater than 97% as determined by SDS-PAGE and SEC-HPLC analyses.
Biological Activity
Immobilized Recombinant Human AMH at 3 µg/mL (100 µL/well) will bind Recombinant Human MIS RII Fc Chimera with a linear range of 2.0-100 ng/mL. The activity was measured by its binding ability in a functional ELISA.More Info
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Introduction
Anti-Mullerian Hormone also known as AMH is a member of the TGF-beta family. AMH is a glycoprotein which is produced by the Sertoli cells of the testis, causes regression of the Muellerian duct. AMH inhibits the growth of tumors derived from tissues of Muellerian duct origin. Moreover, AMH participates in Leydig cell differentiation and function in addition to follicular development in adult females.
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Synonyms
Anti-Muellerian hormone, AMH, Muellerian-inhibiting substance, MIS, MIF.
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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; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to reconstitute in sterile 4mM HCl to a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SAGATAADGP CALRELSVDL RAERSVLIPE TYQANNCQGV CGWPQSDRNP RYGNHVVLLL KMQVRGAALA RPPCCVPTAY AGKLLISLSE ERISAHHVPN MVATECGCR.
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 Human RecombinantDescription:
c-Reactive Protein Human Recombinant
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
Product # :
PRO-335Price :
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Shipped with Ice Packs
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Description
Recombinant Human CRP produced in E.Coli is a non-glycosylated polypeptide chain having a total molecular mass of 115 kDa that corresponds to the pentamer structure of 23 kDa monomer determined by amino acid sequence. The CRP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The sterile protein solution contains 20mM Tris (pH 7.5), 2mM CaCl2, 0.14M NaCl and 0.05% NaN3.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
sds-page
More Info
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Introduction
CRP is an acute phase protein that correlates with inflammatory disease and is synthesized by hepatocytes during the acute phase response by certain cytokines (IL-1 and TNF Alpha and Beta). CRP levels increase dramatically (up to 1,000 fold) and serve as a useful marker of inflammation in such conditions as bacterial infection, rheumatoid arthritis, viral infections, transplantation rejection, meningitis, myocardial infarction, septicemia, osteomyelitis and others. CRP is also highly correlated to Serum Amyloid A levels.
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Synonyms
C-reactive protein, CRP, PTX1, MGC88244, MGC149895.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
CRP should be stored at all times at 4°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.
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Name :
Cyclophilin A E.ColiDescription:
Cyclophilin A E.Coli Recombinant
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, CypA, rot, rotA.
Product # :
ENZ-859Price :
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Description
Cyclophilin A E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (25-190a.a.) and having a molecular mass of 20.5kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
Cyclophilin A protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.
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Synonyms
Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, CypA, rot, rotA.
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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 MGSAKGDPHV LLTTSAGNIE LELDKQKAPV SVQNFVDYVN SGFYNNTTFH RVIPGFMIQG GGFTEQMQQK KPNPPIKNEA DNGLRNTRGT IAMARTADKD SATSQFFINV ADNAFLDHGQ RDFGYAVFGK VVKGMDVADK ISQVPTHDVG PYQNVPSKPV VILSAKVLP.
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 :
Cyclophilin D Human, HisDescription:
Cyclophilin-D Human Recombinant, His Tag
Peptidylprolyl isomerase D, PPID, CYPD, CYP-40, 40 kDa peptidyl-prolyl cis-trans isomerase, PPIase, Rotamase, Cyclophilin-40, CYP40, Cyclophilin-related protein, MGC33096, EC 5.2.1.8.
Product # :
ENZ-367Price :
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Description
Cyclophilin-D Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (amino acids 1-370) containing 390 amino acids and having a molecular mass of 42.9kDa. Cyclophilin-D is fused to a 20 aa His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1mg/ml solution containing 1x PBS pH-7.4 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 700 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.
More Info
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Introduction
Cyclophilin-D is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-D possess PPIase activity and binds to the immunosuppressant cyclosporin-A. Cyclophilin-D is very well known that its overexpression suppresses the apoptosis in cancer cell. Cyclophilin-D suppresses apoptotic cell death by the use of mitochondrial hexokinase-2 dependent mechanism in cancer cells.
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Synonyms
Peptidylprolyl isomerase D, PPID, CYPD, CYP-40, 40 kDa peptidyl-prolyl cis-trans isomerase, PPIase, Rotamase, Cyclophilin-40, CYP40, Cyclophilin-related protein, MGC33096, EC 5.2.1.8.
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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 MSHPSPQAKP SNPSNPRVFFDVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGIGH TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDREGLLSMANAGRNTNGS QFFITTVPTP HLDGKHVVFG QVIKGIGVAR ILENVEVKGEKPAKLCVIAE CGELKEGDDG GIFPKDGSGD SHPDFPEDAD IDLKDVDKIL LITEDLKNIG NTFFKSQNWE MAIKKYAEVL RYVDSSKAVI ETADRAKLQPIALSCVLNIG ACKLKMSNWQ GAIDSCLEAL ELDPSNTKAL YRRAQGWQGLKEYDQALADL KKAQGIAPED KAIQAELLKV KQKIKAQKDK EKAVYAKMFA.
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 :
CSRP2 HumanDescription:
Cysteine and Glycine-rich Protein 2 Human Recombinant
Cysteine and glycine-rich protein 2, Smooth muscle cell LIM protein, LIM domain only 5 smooth muscle, SmLIM, LMO5, CRP2.
Product # :
PRO-1096Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
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Description
CSRP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 217 amino acids (1-193) and having a molecular mass of 23.5kDa.CSRP2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CSRP2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
CSRP2 belongs to the CSRP family. CSRP2 holds 2 LIM zinc-binding domains that take part in regulatory processes essential for development and cellular differentiation. Additionally, CSRP2 is involved in the development of the embryonic vascular system.
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Synonyms
Cysteine and glycine-rich protein 2, Smooth muscle cell LIM protein, LIM domain only 5 smooth muscle, SmLIM, LMO5, CRP2.
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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 MGSHMPVWGG GNKCGACGRT VYHAEEVQCD GRSFHRCCFL CMVCRKNLDS TTVAIHDEEI YCKSCYGKKY GPKGYGYGQG AGTLNMDRGE RLGIKPESVQ PHRPTTNPNT SKFAQKYGGA EKCSRCGDSV YAAEKIIGAG KPWHKNCFRC AKCGKSLEST TLTEKEGEIY CKGCYAKNFG PKGFGYGQGA GALVHAQ
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 :
PI3 HumanDescription:
Peptidase Inhibitor 3 Human Recombinant
Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 3.
Product # :
PRO-1627Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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Description
PI3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (23-117) and having a molecular mass of 12.0kDa.PI3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PI3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
PI3 is an elastase-specific protease inhibitor, which contains a WAP-type four-disulfide core (WFDC) domain, and is thus a member of the WFDC domain family. Most WFDC gene members are localized to chromosome 20q12-q13 in two clusters: centromeric and telomeric. PI3 belongs to the centromeric cluster.
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Synonyms
Peptidase Inhibitor 3 Skin-Derived, Skin-Derived Antileukoproteinase, Protease Inhibitor 3 Skin-Derived (SKALP), WAP Four-Disulfide Core Domain Protein 14, WAP Four-Disulfide Core Domain 14, Elastase-Specific Inhibitor, Protease Inhibitor WAP3, ESI, trappin-2, cementoin, WFDC14, WAP3, elafin, pre-elafin, SKALP, Peptidase Inhibitor 3.
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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 MGSAVTGVPV KGQDTVKGRV PFNGQDPVKG QVSVKGQDKV KAQEPVKGPV STKPGSCPII LIRCAMLNPP NRCLKDTDCP GIKKCCEGSC GMACFVPQ
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 :
CKBB HumanDescription:
Creatine Kinase Brain Human Recombinant
Creatine kinase B-type, B-CK, BCK, CKBB, HEL-211, HEL-S-29, CKB, EC 2.7.3.2, Creatine kinase B chain, CKB, CKBB, CKBBI.
Product # :
PKA-089Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
CKBB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-381a.a) and having a molecular mass of 42.6kDa. CKB is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CKBB solution (1mg/ml) contains 20mM Tris-Hcl Buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
CKBB purity was found to be greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Creatine Kinase BB is a cytoplasmic enzyme involved in energy homeostasis. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in brain as well as in other tissues, and as a heterodimer with a similar muscle isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. A pseudogene of this gene has been characterized.
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Synonyms
Creatine kinase B-type, B-CK, BCK, CKBB, HEL-211, HEL-S-29, CKB, EC 2.7.3.2, Creatine kinase B chain, CKB, CKBB, CKBBI.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire CKBB 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
MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K.
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.