Recombinant Human Multifunctional procollagen lysine hydroxylase and glycosyltransferase LH3 (PLOD3)

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Code CSB-MP018201HU
MSDS
Size $660
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
PLOD3
Uniprot No.
Research Area
Others
Alternative Names
2-oxoglutarate 5-dioxygenase 3; bone protein I; BP-I; LH3; Lysine hydroxylase 3; Lysyl hydroxylase 3; Plod3; PLOD3_HUMAN; Procollagen lysine,2 oxoglutarate 5 dioxygenase 3 precursor; Procollagen-lysine
Species
Homo sapiens (Human)
Source
Mammalian cell
Expression Region
25-738aa
Target Protein Sequence
SDRPRGRDPVNPEKLLVITVATAETEGYLRFLRSAEFFNYTVRTLGLGEEWRGGDVARTVGGGQKVRWLKKEMEKYADREDMIIMFVDSYDVILAGSPTELLKKFVQSGSRLLFSAESFCWPEWGLAEQYPEVGTGKRFLNSGGFIGFATTIHQIVRQWKYKDDDDDQLFYTRLYLDPGLREKLSLNLDHKSRIFQNLNGALDEVVLKFDRNRVRIRNVAYDTLPIVVHGNGPTKLQLNYLGNYVPNGWTPEGGCGFCNQDRRTLPGGQPPPRVFLAVFVEQPTPFLPRFLQRLLLLDYPPDRVTLFLHNNEVFHEPHIADSWPQLQDHFSAVKLVGPEEALSPGEARDMAMDLCRQDPECEFYFSLDADAVLTNLQTLRILIEENRKVIAPMLSRHGKLWSNFWGALSPDEYYARSEDYVELVQRKRVGVWNVPYISQAYVIRGDTLRMELPQRDVFSGSDTDPDMAFCKSFRDKGIFLHLSNQHEFGRLLATSRYDTEHLHPDLWQIFDNPVDWKEQYIHENYSRALEGEGIVEQPCPDVYWFPLLSEQMCDELVAEMEHYGQWSGGRHEDSRLAGGYENVPTVDIHMKQVGYEDQWLQLLRTYVGPMTESLFPGYHTKARAVMNFVVRYRPDEQPSLRPHHDSSTFTLNVALNHKGLDYEGGGCRFLRYDCVISSPRKGWALLHPGRLTHYHEGLPTTWGTRYIMVSFVDP
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
85.9 kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 10xHis-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
Tris-based buffer,50% glycerol
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

Function
Multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen. Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine. Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen-like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5-hydroxylysine residues. Essential for normal biosynthesis and secretion of type IV collagens. Essential for normal formation of basement membranes.
Gene References into Functions
  1. VIPAR, with its partner proteins, regulate sorting of lysyl hydroxylase 3 (LH3, also known as PLOD3) into newly identified post-Golgi collagen IV carriers PMID: 27435297
  2. Proteomic analysis revealed that PLOD3, which is the gene encoding for collagen-modifying lysyl hydroxylase 3 (LH3), is regulated by miR-663a. PMID: 27233793
  3. The study shows that lysyl hydroxylase 3 localizes to epidermal basement membrane and is reduced in patients with recessive dystrophic epidermolysis bullosa. PMID: 26380979
  4. MMP-9 recruitment to the fibroblast cell surface by Lysyl Hydroxylase 3 (LH3) triggers TGF-beta activation and fibroblast differentiation PMID: 25825495
  5. LH3 molecules found in the cell medium are secreted through the Golgi complex, and the secretion is dependent on LH3 glycosyltransferase activity; LH3 found on the cell surface bypasses the Golgi complex PMID: 21465473
  6. Dimerization of human lysyl hydroxylase 3 is mediated by the amino acids 541-547 PMID: 20955792
  7. Characterization of three fragments that constitute the monomers of the human lysyl hydroxylase isoenzymes 1-3. The 30-kDa N-terminal fragment is not required for lysyl hydroxylase activity PMID: 11956192
  8. Manipulation of the gene for LH3 can be used to selectively alter glycosylation and hydroxylation reactions, and provides new tool to clarify functions of unique hydroxylysine linked carbohydrates in collagens and other proteins. PMID: 12475640
  9. LH3 is present and active in the extracellular space PMID: 16447251
  10. The deficiency of LH3 glycosyltransferase activities, especially in the extracellular space, causes growth arrest. PMID: 18298658
  11. mutations of the lysyl hydroxylase 3 gene may cause a connective tissue disorder [case report] PMID: 18834968

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Involvement in disease
Lysyl hydroxylase 3 deficiency (LH3 deficiency)
Subcellular Location
Rough endoplasmic reticulum. Endoplasmic reticulum lumen. Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. Secreted. Secreted, extracellular space.
Tissue Specificity
Ubiquitous. Detected in heart, placenta and pancreas and at lower levels in lung, liver and skeletal muscle.
Database Links

HGNC: 9083

OMIM: 603066

KEGG: hsa:8985

STRING: 9606.ENSP00000223127

UniGene: Hs.153357

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